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lipA

Gene
lipA
Protein
Capsule polysaccharide modification protein LipA
Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Length
704 amino acids
Function
Involved in the phospholipid modification of the capsular polysaccharide, a strong requirement for its translocation to the cell surface.
Mass
79.566 kDa
Sequence
MFLFSDGLQSINNNNRRKRIVKNAYIPSRGIRKIPHLSTLLPEFHIYKDGKGAEAVVGWGLRPTTHKARAFATEHQLPFIALEDGFLRSLGLGVSGYPPYSIVYDDIGIYYDTTRPSRLEQLILAADTMPSETLAQARQAMDFILQHHLSKYNHAPELSDDHPLRSPSKSETVLIIDQTFGDMAIQYGGADASTFELMFQTALNENPQADIWVKTHPDVLCGKKQGYLTQLVQQHRVHLLAEDINPISLLQNVDKVYCVTSQMGFEALLCGKPLTTFGLPWYAGWGVSDDRHPKIGSLIQTQRRAPRNLLQLFAAAYLQYSRYLNPNTGEAGSLFDVIDYLATVKRKNDKLRGELYCVGMSLWKRAVAKPFFNVPSCRLKFISSTQKLARVKLSDDARILAWGNGKEAIVRFAEQHHIPLLRMEDGFIRSVGLGSNLVPPLSLVTDDMSIYFNAETPSRLEYILQNQNFDDQDFQTALKLQKMLTENHISKYNVGSSDFTAPSTDKTVILVPGQVEDDASIRYGSPQIYRNLDLLRTVRERNPNAYIIYKPHPDVVSGNRIGHISPDDAARYADQTAEQADILTCLQYADEIHTMTSLTGFEALLRGKKVSCYGLPFYAGWGLTQDLLPIPRRSRRLELWQLVAGTLIYYPDYIHPKTHQAINAETAAQILIRQKNMQKNNNGLHRGCFAKKLGKIKQLYRSFK

Gene
lipA
Protein
Capsule polysaccharide modification protein LipA
Organism
Neisseria meningitidis serogroup B (strain MC58)
Length
704 amino acids
Function
Involved in the phospholipid modification of the capsular polysaccharide, a strong requirement for its translocation to the cell surface.
Mass
79.606 kDa
Sequence
MFLFSDGLQSINNNNRRKRIVKNAYIPSRGIRKIPHLSTLLPEFHICKDGKEAEAVVGWGLRPTTHKARAFAAEHQLPFIALEDGFLRSLGLGVAGYPPYSIVYDDIGIYYDTTRPSRLEQLILAADTMPSETLAQAQQAMDFILQHHLSKYNHAPELSDDHPLRSPSKPETVLIIDQTFGDMAIQYGGADASTFELMFQTALNENPQADIWVKTHPDVLCGKKQGYLTQLAQQHRVHLLAEDINPISLLQNVDKVYCVTSQMGFEALLCGKPLTTFGLPWYAGWGVSDDRHPEINRLVQTQRRATRNLLQLFAAAYLQYSRYLNPNTGEAGSLFDVIDYLATVKRKNDKLRGELYCVGMSLWKRAVAKPFFNVPSCRLKFISSTQKLARVKLSDDARILAWGNGKEAIVRFAEQHHIPLLRMEDGFIRSVGLGSNLVPPLSLVTDDMSIYFNAETPSRLEYILQNQNFDDQDFQTALKLQKMLTENHISKYNVGSSDFTAPSTDKTVILVPGQVEDDASIRYGSPQIYRNLDLLRTVRERNPNAYIIYKPHPDVVSGNRIGHISPEDAARYADQTAEQADILTCLQYADEIHTMTSLTGFEALLRGKKVSCYGLPFYAGWGLTQDLLPIPRRSRRLELWQLIAGTLIHYPDYIHPETHQAINAETAAQILIRQKNMQKNNNGLHRGCFAKKLGKIKQLYRSFK

Gene
lipA
Protein
Lipase 1
Organism
Staphylococcus aureus (strain NCTC 8325)
Length
680 amino acids
Similarity
Belongs to the AB hydrolase superfamily. Lipase family.
Mass
76.675 kDa
Sequence
MKSQNKYSIRKFSVGASSILIATLLFLSGGQAQAAEKQVNMGNSQEDTVTAQSIGDQQTRENANYQRENGVDEQQHTENLTKNLHNDKTISEENHRKTDDLNKDQLKDDKKSSLNNKNIQRDTTKNNNANPSDVNQGLEQAINDGKQSKVASQQQSKEADNSQDSNANNNLPSQSRIKEAPSLNKLDQTSQREIVNETEIEKVQPQQNNQANDKITNYNFNNEQEVKPQKDEKTLSVSDLKNNQKSPVEPTKDNDKKNGLNLLKSSAVATLPNKGTKELTAKAKDDQTNKVAKQGQYKNQDPIVLVHGFNGFTDDINPSVLAHYWGGNKMNIRQDLEENGYKAYEASISAFGSNYDRAVELYYYIKGGRVDYGAAHAAKYGHERYGKTYEGIYKDWKPGQKVHLVGHSMGGQTIRQLEELLRNGNREEIEYQKKHGGEISPLFKGNHDNMISSITTLGTPHNGTHASDLAGNEALVRQIVFDIGKMFGNKNSRVDFGLAQWGLKQKPNESYIDYVKRVKQSNLWKSKDNGFYDLTREGATDLNRKTSLNPNIVYKTYTGEATHKALNSDRQKADLNMFFPFVITGNLIGKATEKEWRENDGLVSVISSQHPFNQAYTKATDKIQKGIWQVTPTKHDWDHVDFVGQDSSDTVRTREELQDFWHHLADDLVKTEKLTDTKQA

Gene
lipA
Protein
Lipoprotein A
Organism
Mycoplasma pulmonis (strain UAB CTIP)
Length
578 amino acids
Similarity
Belongs to the M.pulmonis LipAB lipoprotein family.
Mass
66.219 kDa
Sequence
MNKKYFKKYSWVLILSTSILAPMTLASCNHNVAKKEDKTQNDSSNLSNKTNKSDPNDHLKDKDKNVSQDNKDSTNKAVSNENSQTQSQKTNESSQNTKDDSSKTSNLITNQNSSSNTKSKIQENKQSQKDQNTSAVNVSALEKQTKNDENISLVNSKDTNVILKNDEKVALAKDDSKEKSKNSSNLNLKTPVENRQNKNEVKDDKKALQWWQKLNESASILESFSYDQTSLSLTFKEGMPLGLEVVLKLENLDSHEEKEISFKTTNGKVQNVLLTSSNLTSGKWKIKSFSFDKTYSHSPTIETTFDFKTNEKLKQERIEKIQKAIDKYQIKIKQNYKDKPLISKYALSNFDLNLNFKDLEIVNNSLKFDGSNLNQDLKSEKQMKITFEKVSENQANKTRKAHFKITTLDNLVFEKTLEWSYKTNKEYLDEFKNGSALWDDLQASLTSVFEKSLWHPYQLPKAKSKINTINLINDVSASFQGYDYLDDFNGSAKLKFKLQRGQEQRDITFTINGFLKVSLIDPLYKGNLRNSEFDVKASSNGYWLGQYYTAAEVFKHYSNGKSYWYATANDGNPWLEFS

Gene
lipA
Protein
Lipoyl synthase, apicoplast
Organism
Toxoplasma gondii
Length
543 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
58.706 kDa
Sequence
MAYFFDFPTDTWVEDASPGGPPKRAFGHGLAAGSSHFASPVSRRRLPTITALLLFSLLSASQSGALSVSQCSRRVSLGPLLSRVSSVSCTPSAAASALASSLYPTDSLSSVEGSVAPRPPPSSLAFVLRRVPPAAYSSSLSPSVLRFKHSLPRPLQGSLVCAPGILGGAAGSARFAGCCGSQGRSCGSGKNPELPLKGSKDEVIPRVGTSTAGPRPDWFHVPAPQAASRGAEESRYQQLQKQIRGLDLHTVCEEAKCPNIGECWNGGTATLILLGDTCTRGCRFCAIKTSSKPPPPDPLEPEKVADAVAKWDIDYVVMTSVDRDDMPDGGAGHFARTVQLVKKAKPSMLIECLVSDFQGMEESVRTLAQSGLDVYAHNIETVRRLTPYVRDKRAKYDQSLRVLHLAKQFNPSLFTKSSIMLGLGETSEEVVRTLRDLRDHDVDVVTLGQYLRPTKQQLGVVEYVTPETFKKYQDIAEEMGFKYVASGPLVRSSYKAGEYYMKHLIDDARKHGRRETVKQVKLEADVGTLKGTTTTFQVNEKEA

Gene
lipA
Protein
Lipoyl synthase, apicoplast
Organism
Plasmodium yoelii yoelii
Length
502 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
57.463 kDa
Sequence
MNFLVLFFSYSIFVLPYSILVYGISKDRKCCEYGNSVDSSKILYIAGSVRKRRKTFEKKINVSNFEREGNANGYKHIDNKGIYATKQNLEFDEARNKEANENNKNDATTVNRKIIIESENKNNHNNQEQNIKDCYTNENAQNDEKNKKVKIPKVGNAMPEKKPDWFHVPAPNGEKYKKLKSDLGKLKLHTVCEEAQCPNIGECWNIGTATIMLLGDTCTRGCKFCSIKTSSKPPPPDINEPFNTAKAICEWDINYIVITSVDRDDLPDGGADHFAKTVELIKFSKPSILIECLVSDFQGNIDSIKRLALSGLDVYAHNIETVKRLQKYVRDKRANYEQSLYVLKKAKEINPNLYTKTSIMLGLGETQDEVLQTMKDARSNDIDVITFGQYLRPTKNHLNVVEYISPQMFNYYKDVGLKMGFKYIASGPLVRSSYMAGEYFMKNMVEKGRNQKNQQIKPVELKLVTELDKLTECIQKEIKHREISVFIQVHAFLVNVFVLVRA

Gene
lipA
Protein
Lipoyl synthase, apicoplast
Organism
Plasmodium knowlesi (strain H)
Length
442 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
50.641 kDa
Sequence
MRVLTPSLYIYAFFIFCVRFKCGNRTTVASAIRASYDMPPKELRVGDMLKKTSQPNCNYRTRGKCRKFFFVWKLDKMRDAHLGVQAKRRKNHLRSGSATYEASLGEHQLKGKRKESATNVEKEKKEKEQQEERLPVPKVGNKMPEKKPDWFHVPAPTGKKYNKLKEDLKKLKLHTVCEEAQCPNIGECWNIGTATIMLLGDTCTRGCKFCSIKTSSKPLAPDANEPFNTAKAICEWDINYVVLTSVDRDDLPDGGASHFAKTIELIKFSRPEILIECLVSDFQGNVDSIRKLANSGMEVYAHNIETVRRLQKFVRDRRANYEQSLRVLKIAKEINPMLYTKTSIMLGLGETKEEVLEAMSDVRQHNIDVITFGQYLRPTKNHLNVVEYVSPQMFDFYKEEGMKMGFKYIASGPLVRSSYKAGEYFMKSLVEQRRGAKTHAQG

Gene
lipA
Protein
Lipoyl synthase, apicoplast
Organism
Plasmodium vivax (strain Salvador I)
Length
442 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
50.317 kDa
Sequence
MHVLTPSLYIYAFFIVCVRLKCGRSKRVANAKHATYDMPPKGLRVRDMLEKTAQQNCNQRKRGKCRKFFFLWKMDKMGDTHLGGQANGRKNLLRSESATDEASLGGNPLKEKLKESPANWGKDKQEEQQSTDRLPLPKVGNKMPEKKPDWFHVPAPTGKKYNELKADLKKLKLHTVCEEAQCPNIGECWNIGTATIMLLGDTCTRGCKFCSIKTSSKPLPPDANEPFNTAKAICEWDINYVVLTSVDRDDLPDGGASHFAKTIELIKFSRPEILIECLVSDFQGNVDSIRKLANSGMEVYAHNIETVRRLQKFVRDRRANYEQSLWVLKTAKEINPLLYTKTSIMLGLGETKQEVLQAMADVRQNNIDVITFGQYLRPTKNHLNVVEYVSPQMFDYYKEEGMKMGFKYIASGPLVRSSYKAGEYFMKNLVEQRRGVKLHAEG

Gene
lipA
Protein
Lipase A
Organism
Acremonium alcalophilum
Length
416 amino acids
Function
Lipolytic enzyme that possesses both lipase and acetylxylan esterase activity. Active towards p-nitrophenol esters of various carbon chain length with preference for medium-chain fatty acids (C-8). Also highly active on the acetylated compounds xylose tetra-acetate and oat spelt xylan.
Similarity
Belongs to the AB hydrolase superfamily. Lipase family.
Mass
45.645 kDa
Sequence
MRLAPQKPLLLSTVLHLLLSIWMLGFASLAGATVQEPLAASDTPKPVSAALFSSIERLSRLVDITYCVGNTGVWKPFACASRCNEFPTLTLERTWRTGILMSDSCGLIAVDHGTPRHDAGEGKDDPLAEKAIIVAFRGTYSLTNTIIDLSTIPQEYVPYPSPDDGGNEPPREPSHRCDNCTVHSGFLASWRHARKVVLPELKVLRQKYPEYPIRLVGHSLGGAVAMLAALEMRVSLGWRDTVVTTFGEPRVGNRQLCDYLNAVFELNLGDEMDPAEREYRRVTHADDPVPLLPPAEWGYSSHGGEFFISKKDLPPSVEDVLVCHGDHDENCIARGKSSAVSVPAGDYDDALSTLEEQDVMLADALPWIPARLKLWELFFAHRDYFWRLGLCVPGGDPANWGRKGGEGAAESISAEG

Gene
lipA
Protein
Lipase A
Organism
Acremonium alcalophilum
Length
416 amino acids
Function
Lipolytic enzyme that possesses both lipase and acetylxylan esterase activity. Active towards p-nitrophenol esters of various carbon chain length with preference for medium-chain fatty acids (C-8). Also highly active on the acetylated compounds xylose tetra-acetate and oat spelt xylan.
Similarity
Belongs to the AB hydrolase superfamily. Lipase family.
Mass
45.645 kDa
Sequence
MRLAPQKPLLLSTVLHLLLSIWMLGFASLAGATVQEPLAASDTPKPVSAALFSSIERLSRLVDITYCVGNTGVWKPFACASRCNEFPTLTLERTWRTGILMSDSCGLIAVDHGTPRHDAGEGKDDPLAEKAIIVAFRGTYSLTNTIIDLSTIPQEYVPYPSPDDGGNEPPREPSHRCDNCTVHSGFLASWRHARKVVLPELKVLRQKYPEYPIRLVGHSLGGAVAMLAALEMRVSLGWRDTVVTTFGEPRVGNRQLCDYLNAVFELNLGDEMDPAEREYRRVTHADDPVPLLPPAEWGYSSHGGEFFISKKDLPPSVEDVLVCHGDHDENCIARGKSSAVSVPAGDYDDALSTLEEQDVMLADALPWIPARLKLWELFFAHRDYFWRLGLCVPGGDPANWGRKGGEGAAESISAEG

Gene
lipA
Protein
Lipoyl synthase, apicoplast
Organism
Plasmodium falciparum (isolate 3D7)
Length
415 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
47.593 kDa
Sequence
MHFGIPSLFYLYILFSIIMRIKCVITKNLKKTKKRTCSYIPHGNMEKGIILNYIEKPNPAYLKRGKNKNKNKNKKGDIYKLRNVEILLYANRYVHEGNENFSSTTKKLLLTPKVGNKMPEGKKPDWFHVAAPTVAKYNKLKDDIKKLNLHTVCEEAQCPNIGECWNIGTATIMLLGDTCTRGCKFCSIKTSSNPLPPDINEPFNTAKAICEWNIDYVVLTSVDRDDLPDGGASHFAKTVELVKFSRPDILIECLVSDFQGNIDSVRKLAFSGLDVYAHNIETVKRLQKYVRDKRANYDQSLFVLKTAKEINPQLYTKTSIMLGLGETKEEVIQTMYDARKNNIDVITFGQYLRPTKNHLSIVQYISPQMFEYYKEEGLKMGFKYIASGPLVRSSYKAGEYFIKNLVNQRNKDKKN

Gene
LIPA
Protein
Lysosomal acid lipase/cholesteryl ester hydrolase
Organism
Homo sapiens
Length
399 amino acids
Function
Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation.
Similarity
Belongs to the AB hydrolase superfamily. Lipase family.
Mass
45.419 kDa
Sequence
MKMRFLGLVVCLVLWTLHSEGSGGKLTAVDPETNMNVSEIISYWGFPSEEYLVETEDGYILCLNRIPHGRKNHSDKGPKPVVFLQHGLLADSSNWVTNLANSSLGFILADAGFDVWMGNSRGNTWSRKHKTLSVSQDEFWAFSYDEMAKYDLPASINFILNKTGQEQVYYVGHSQGTTIGFIAFSQIPELAKRIKMFFALGPVASVAFCTSPMAKLGRLPDHLIKDLFGDKEFLPQSAFLKWLGTHVCTHVILKELCGNLCFLLCGFNERNLNMSRVDVYTTHSPAGTSVQNMLHWSQAVKFQKFQAFDWGSSAKNYFHYNQSYPPTYNVKDMLVPTAVWSGGHDWLADVYDVNILLTQITNLVFHESIPEWEHLDFIWGLDAPWRLYNKIINLMRKYQ

Gene
LIPA
Protein
Lysosomal acid lipase/cholesteryl ester hydrolase
Organism
Macaca fascicularis
Length
399 amino acids
Function
Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation (By similarity).
Similarity
Belongs to the AB hydrolase superfamily. Lipase family.
Mass
45.48 kDa
Sequence
MKMRFLGLVVCLVLWTLHSEASGGKLTAVNPETNMNVSEIISYWGFPSEEYLVETEDGYILCLNRIPHGRKNHSDKGPKPVVFLQHGLLADSSNWVTNLANSSLGFILADAGFDVWMGNSRGNTWSRKHKTLSVSQDEFWAFSYDEMAKYDLPASINFILNKTGQEQVYYVGHSQGTTIGFIAFSQIPELAKRIKMFFALAPVVSVDFCTSPMAKLGRLPDLLIKDLFGDKEFLPQSAFLKWLGTHVCTHVILKELCGNLCFLLCGFNERNLNMSRVDVYTTHSPAGTSVQNMLHWSQAVKFQKFQAFDWGSSAKNYFHYNQSYPPTYNVKDMLVPTAVWSGGHDWLADVYDINILLTQITNLVFHESIPEWEHLDFIWGLDAPWRLYNKIINLMKKYQ

Gene
Lipa
Protein
Lysosomal acid lipase/cholesteryl ester hydrolase
Organism
Mus musculus
Length
397 amino acids
Function
Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation (By similarity).
Similarity
Belongs to the AB hydrolase superfamily. Lipase family.
Mass
45.325 kDa
Sequence
MQLQGLVFVFTIGILLSRVPTGTVSAVDPEVNMNVTEIIMRWGYPGEEHSVLTGDGYILSIHRIPRGRKNHFGKGPRPVVYLQHGLLADSSNWVTNIDNSSLGFLLADAGFDVWMGNSRGNTWSLKHKTLSVSQDEFWAFSFDEMAKYDLPASINYILNKTGQEQIYYVGHSQGCTIGFIAFSQMPELAKKIKMFLVLAPVLSLNFASGPLLQLGRLPDPLLKDMFGQKQFLPQSAMLKWLSIHVCTHVIMKELCANVFFLLCGFNEKNLNMSRVDVYTTHCPAGTSVQNMLHWGQVFKYRKLQAFDWGSSEKNYFHYNQSFPPSYNIKNMRLPTALWSGGRDWLADINDITILLTQIPKLVYHKNIPEWDHLDFIWGLDAPWKLYDEIISLMKKYQ

Gene
Lipa
Protein
Lysosomal acid lipase/cholesteryl ester hydrolase
Organism
Rattus norvegicus
Length
397 amino acids
Function
Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation (By similarity).
Similarity
Belongs to the AB hydrolase superfamily. Lipase family.
Mass
45.186 kDa
Sequence
MQLLGRVICFVVGILLSGGPTGTISAVDPEANMNVTEIIMHWGYPEHSVQTGDGYILGVHRIPHGRKNQFDKGPKPVVYLQWRHGFLADSSNWVTNIDNNSLGFILADAGFDVWMGNSRGNTWSRKHKTLSVSQDEYWAFSFDEMAKYDLPASINYILNKTGQEQLYNVGHSQGCTIGFIAFSQMPELAKKVKMFFALAPVLSLNFASGPMVKLGRLPDLLLEDLFGQKQFLPQSAMVKWLSTHICTHVIMKELCANIFFLICGFNEKNLNMSRVDVYTTHCPAGTSVQNMVHWTQVVKYHKLQAFDWGSSDKNYFHYNQSYPPLYSIKDMQLPTALWSGGKDWLADTSDINILLTEIPTLVYHKNIPEWDHLDFIWGLDAPWRLYNEVVSLMKKYQ

Gene
lipA
Protein
Lipoyl synthase
Organism
Xylella fastidiosa (strain M23)
Length
373 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
41.126 kDa
Sequence
MTQPIIRSIPLHVVSNDHPSSSPLQPGVKQSGEDKIGRSPVQFADVPVLRKPSWIRVRIPSGNAVQSLKAKLRENRLVTVCEEAACPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDPEEPISLARTVAEMGLKYVVVTSVDRDDLRDGGAQHFVDCIAAIRQSAPQTRIEILTPDFRGKGRMDRALDILAACPPDVFNHNVETVPALYPNVRPGADYQWSLTLLKRFKAQHPQVPTKSGIMLGLGETLDQVQATLRDLRAHDVDMVTVGQYLQPTPHHHPVLRYWTPDEYKALEEYGMALGFSHVASGPMVRSSYHADHQAKEAGLGFNATVSLGSPAVSSTEHRERNTIASKSASKTESIHHR

Gene
lipA
Protein
Lipoyl synthase
Organism
Xylella fastidiosa (strain 9a5c)
Length
373 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
41.158 kDa
Sequence
MTQPIVRSIPLHVVSNDHPSSSPLQPGVKQSGEDKIGRSPVQFADVPVLRKPSWIRVRIPSGNAVQSLKAKLRENRLVTVCEEAACPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDPEEPISLARTVAEMGLKYVVVTSVDRDDLRDGGAQHFVDCIAAIRQSAPQTRIEILTPDFRGKGRMDRALDILAACPPDVFNHNVETVPALYPNVRPGADYQWSLTLLKRFKAQHPQVPTKSGIMLGLGETLDQVQATLRDLRAHDVDMVTIGQYLQPTSHHHPVLRYWTPDEYKALEEYGMALGFSHVASGPMVRSSYHADHQAKEAGLGFNATVSLGSPAVSSTEHRERHTIASKSASKTESIRHR

Gene
lipA
Protein
Lipoyl synthase
Organism
Xylella fastidiosa (strain M12)
Length
373 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
41.085 kDa
Sequence
MTQPIVRSIPLHVVSNDHPSSSPLQPGVKQSGEDKIGRSPVQFADVPVLRKPSWIRVRIPSGNAVQSLKAKLRENRLVTVCEEAACPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDPEEPISLARTVAEMGLKYVVVTSVDRDDLRDGGAQHFVDCIAAIRQSAPQTRIEILTPDFRGKGRMDRALDILAACPPDVFNHNVETVPALYPNVRPGADYQWSLTLLKRFKAQHPQVPTKSGIMLGLGETLDQVQATLRDLRAHDVDMVTVGQYLQPTSHHHPVLRYWTPDEYKALEEYGMALGFSHVASGPMVRSSYHADHQAKEAGLGFNATVSLGSPAVSSTEHRERHTIASKSASKTESIPHR

Gene
lipA
Protein
Lipoyl synthase
Organism
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Length
373 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
41.126 kDa
Sequence
MTQPIIRSIPLHVVSNDHPSSSPLQPGVKQSGEDKIGRSPVQFADVPVLRKPSWIRVRIPSGNAVQSLKAKLRENRLVTVCEEAACPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDPEEPISLARTVAEMGLKYVVVTSVDRDDLRDGGAQHFVDCIAAIRQSAPQTRIEILTPDFRGKGRMDRALDILAACPPDVFNHNVETVPALYPNVRPGADYQWSLTLLKRFKAQHPQVPTKSGIMLGLGETLDQVQATLRDLRAHDVDMVTVGQYLQPTPHHHPVLRYWTPDEYKALEEYGMALGFSHVASGPMVRSSYHADHQAKEAGLGFNATVSLGSPAVSSTEHRERNTIASKSASKTESIHHR

Gene
lipA
Protein
Lipoyl synthase
Organism
Sorangium cellulosum (strain So ce56)
Length
372 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
40.576 kDa
Sequence
MAQFSPKPEWLKVRAPGGDTYHHLKETFRKLDLHTVCEEARCPNVGECWREGTATVMLLGDVCTRGCRFCAVTTGDPRGAVDVREPEHVARAIARLSLQYVVMTMVNRDDLLDGGAEHVARTVSRLHALRPDLLIETLVGDFQGHMSAVDMVVDAGPDVFAHNVEVVRRITRVIRDVRSSYDQSLAVLRRAKERQRRLAADAAEAGAPAPRRLTKSSIMVGIGETDDEVLEALRDLREAGVDIVTIGQYLRPSSKHAPVQRFVEPETFAAFERAALEMGFLYAASAPLVRSSYKAAEVFVRSLMDRGGAALPASPGAAAVEALLEERLAVARREAARLTAELDPDEPRPPVAPAPASASPARLVPAASLIRR

Gene
LIPA
Protein
Ligninase A
Organism
Phanerochaete chrysosporium
Length
372 amino acids
Function
Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.
Similarity
Belongs to the peroxidase family. Ligninase subfamily.
Mass
39.394 kDa
Sequence
MAFKQLVAAISLALSLTTANAAVVKEKRATCSNGATVGDASCCAWFDVLDDIQQNLFQGGQCGAEAHESIRLVFHDAIAISPAMEAQGKFGGGGADGSIMIFDDIEPNFHPNIGLDEIINLQKPFVQKHGVTPGAFIAFAGAVALSNCPGAPQMNFFTGRAPATQPAPDGLVPEPFHTVDQIIARVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIFDSQFFVETQFRGILFPGSGGNQGEVESGMAGEIRIQTDHTLARDSRTACEWQSFVNNQSKLVSDFQFIFLALTQLGQDPNAMTDCSDVIPISKPIPGNLPFSFFPPGKSMKDVEQACAETPFPSLVTLPGPATSVARIPPPPGA

Gene
lipA
Protein
Lipoyl synthase
Organism
Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1)
Length
363 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
40.96 kDa
Sequence
MTVKPEGRKMLRIEKKNAESPIEQKPRWIRNQVRTGPGYEDMKSRVTGASLHTVCQEAGCPNIHECWESREATFLIGGDKCTRRCDFCDIATGKPAELDRDEPRRVAENIQEMDLNYTTITGVTRDDLPDEGAWLYAEVVRKIHELNPNTGVENLTPDFSGKPDLLQEVFEARPEVFAHNLETVPRIFKRIRPAFRYERSLDVIRQAHDFGLITKSNLILGMGETAEEIEEALRDLRSAGCDIITITQYLRPGPRFHPIERWVRPEEFVEHSKLAKELGFGGVMSGPLVRSSYRAGRLYVQAMEARGLELPENLKHLAETSQGATAQEASTLLEKYGPSEETPVTTRMAKTPAQSNSVAATIR

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia bellii (strain RML369-C)
Length
355 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.989 kDa
Sequence
MTNLDRHLSKFAYREEFAGNTEVLATAAYKEDCADASTGLTPKLPLEVEFGKMSKRPDWIKVKAPNSSEYYNTKDLIKNLKLNTVCEEAACPNIGECWSKKHATVMILGSVCTRACRFCNVKTGRPDLLDPHEPQRLAEAVQKLGLKHVVITSVDRDDLEDGGATHFAECISEIRKSSPNTTIEILTPDFLRKDGAAEIIANAKPDVFNHNVETVPSLYNTIRPGARYYNSLSLLHNIKKLSPEVFTKSGMMVGLGEEISEVVQVMDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERVARTKGFLMVSASPLTRSSYHADEDFEKLKENYRHRHCEERRSIDVAIS

Gene
lipA
Protein
Lipoyl synthase
Organism
Nocardia farcinica (strain IFM 10152)
Length
352 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
38.871 kDa
Sequence
MTSVDTPTPHGGTPAPAPATANGRKLLRIEARNAQTPIERKPKWIRTRATMGPEYSELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGEQCTRRCDFCQIDTGKPAALDRDEPRRVAESVQAMGLRYSTITGVARDDLEDGGAWLYAETVRAIKRLNPATGVELLIPDFNADPDQLAEVFSARPEVLAHNLETVPRIFKRIRPAFRYERSLSVLTAAREAGLVTKSNLILGMGETPEEVTEAMRDLHEAGCDILTITQYLRPSPRHHPVDRWVKPEEFVEHSRVAEEIGFAGVMAGPLVRSSYRAGRLYAQAMAHHGREIPPAMAHLAEEGTASQEASAVLARFGS

Gene
lipA
Protein
Lipoyl synthase
Organism
Tropheryma whipplei (strain TW08/27)
Length
351 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.596 kDa
Sequence
MNDSGNSSKVNVRPPSAGLGAPSPGKRKMLRLEVRNSQVPIERKPSWIRARATIGTEYRKVQERVKKQNLRTVCQEAGCPNIYECWEDREATFLIGGSQCTRRCDFCQIDTGKPAELDLDEPKRVGQSVAQMKLRYATVTGVARDDLPDGGVWLYAETIREIHKQCPGSGVEILIPDFNGKPELLQQIFEAQPEVYAHNIETVPRIFRRIRPAFRYDRSLDVISQGQKAGMITKSNLILGMGETGEEVTQALRDLKSAGCDIVTITQYLRPSPRHLPVARWVKPQEFIEYKEQAKEIGFSGVLAGPLVRSSYRAGKLWAQSVKAKMVEIPERVRKLINEIEMQETSFRQAV

Gene
lipA
Protein
Lipoyl synthase
Organism
Tropheryma whipplei (strain Twist)
Length
351 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.596 kDa
Sequence
MNDSGNSSKVNVRPPSAGLGAPSPGKRKMLRLEVRNSQVPIERKPSWIRARATIGTEYRKVQERVKKQNLRTVCQEAGCPNIYECWEDREATFLIGGSQCTRRCDFCQIDTGKPAELDLDEPKRVGQSVAQMKLRYATVTGVARDDLPDGGVWLYAETIREIHKQCPGSGVEILIPDFNGKPELLQQIFEAQPEVYAHNIETVPRIFRRIRPAFRYDRSLDVISQGQKAGMITKSNLILGMGETGEEVTQALRDLKSAGCDIVTITQYLRPSPRHLPVARWVKPQEFIEYKEQAKEIGFSGVLAGPLVRSSYRAGKLWAQSVKAKMVEIPERVRKLINEIEMQETSFRQAV

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas mendocina (strain ymp)
Length
350 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
38.651 kDa
Sequence
MSDTSSPKPVASGEKFRTAQGITAIKDGQKRRASAEPQVFEPKPKWLRVKAPGGSRFEAVKRNVGEHRLSTVCQESHCPNMGECWSNGTATIMLMGSVCTRACRFCAVDTGNPNGWLDLEEPQNTAKSVELMALRYIVLTSVDRDDLEDGGASHYAACVRAIKENTPQVVVEALTPDFDGDHQAIERVVDSGLEVFAQNVETVKRLTHVVRDPRAGYEKTLKVLEHAKKHRPQVLTKTSLMLGLGETDEEILETMDDLRAIGVDILTLGQYLQPTRNHLKVQRWVSPEEFNRLRDIGLEKGFMEVAAGPLVRSSYRADRVFEKNNLGLAAPLPVPGQEVDASLIPALNLN

Gene
lipA
Protein
Lipoyl synthase
Organism
Corynebacterium jeikeium (strain K411)
Length
349 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.346 kDa
Sequence
MSVTADGRRMLRIEAKNAETPIESKPRWIRTTAKVGPEYRDIKNRVKGAGLHTVCQEAGCPNINECWEDREATFLIGGDTCSRRCDFCQIKSGRPSPLDMDEPRRVAENVREMGLRYATITGVTRDDLDDEGAWLYAEVVKKIHELNPNTGVENLTPDFSNRPELLKVVFDSQPEVFAHNLETVPRIFKRIRPAFKYDRSLEVIQAAHDYGLVTKSNLILGMGEKKEEVRAAIKDLADAGTDILTITQYLRPSSMHHPIERWVKPEEFMEHSDAAYELGIKAVMSGPLVRSSYRAGRLYAQAKQARGEAIPENLKHLEETLDSTTSQEASTLLERYGASEDTPVTASRR

Gene
lipA
Protein
Lipoyl synthase
Organism
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Length
349 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.123 kDa
Sequence
MTKAPEGRRMLRVEARNSQTPIESKPRWIRTAVKTGPEYQDMKKKVSGASLHTVCQEAGCPNIHECWESREATFLIGGANCSRRCDFCQINSAKPEPLDRDEPRRVAESVREMQLNYSTITGVTRDDLEDEGAWLYAEVVRKIHELNPHTGVENLTPDFSGKPDLLQEVFEARPEVFAHNLETVPRIFKRIRPAFRYERSLDVIRQARDFGLVTKSNLILGMGETVDEIRDALVDLHSAGCDIITITQYLRPGPMYHPIDRWVKPEEFIDHADFARELGFGAVMSGPLVRSSYRAGKLYAEALAARGESLPENLAHLATTADGSTAQEANTLLEKYGPSQDTPVVSSKA

Gene
lipA
Protein
Lipoyl synthase
Organism
Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
Length
348 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
38.55 kDa
Sequence
MSESAKPRITSGSKFRNEHGFSAIKDGVKRSSSNTEGKSLERKPKWLRARMPGGERYDAVRRNVTEHRLSTVCQESHCPNIGECWTNGTATIMVMGSVCTRACKFCAVDTGNPKGWLDPEEPENTAKSVELMGLRYIVLTSVDRDDLPDGGAAHYAACVSAIKQRTPEVAVEALTPDFDAVMSDVEKVVDSGLDVFAQNVETVKRLTSRVRDPRAGYEKTLSVLAHAKKHRPDVLTKTSLMLGLGETEEEILETMDDLRAIGVDILTLGQYLRPTPNHLPVERYVTPEEFNRYRDIGLEKGFMEVPSGPMVRSSYRADRVFDKNNLGLSVPEVPVPDKAMQIPVKAVD

Gene
lipA
Protein
Lipoyl synthase
Organism
Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
Length
348 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
38.55 kDa
Sequence
MSESAKPRITSGSKFRNEHGFSAIKDGVKRSSSNTEGKSLERKPKWLRARMPGGERYDAVRRNVTEHRLSTVCQESHCPNIGECWTNGTATIMVMGSVCTRACKFCAVDTGNPKGWLDPEEPENTAKSVELMGLRYIVLTSVDRDDLPDGGAAHYAACVSAIKQRTPEVAVEALTPDFDAVMSDVEKVVDSGLDVFAQNVETVKRLTSRVRDPRAGYEKTLSVLAHAKKHRPDVLTKTSLMLGLGETEEEILETMDDLRAIGVDILTLGQYLRPTPNHLPVERYVTPEEFNRYRDIGLEKGFMEVPSGPMVRSSYRADRVFDKNNLGLSVPEVPVPDKAMQIPVKAVD

Gene
lipA
Protein
Lipoyl synthase
Organism
Corynebacterium glutamicum (strain R)
Length
348 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.311 kDa
Sequence
MTIAPEGRRLLRVEARNSETPIETKPRWIRNQVKNGPEYQDMKERVAGASLHTVCQEAGCPNIHECWESREATFLIGGANCSRRCDFCMINSARPEPLDRGEPLRVAESVREMQLNYSTITGVTRDDLDDEGAWLYSEVVRKIHELNPHTGVENLVPDFSGKKDLLQEVFESRPEVFAHNVETVPRIFKRIRPAFRYERSLDVIRQARDFGLVTKSNLILGMGETKEEITEALQDLHDAGCDIITITQYLRPGPLFHPIERWVKPEEFLEHADAAKEMGFAAVMSGPLVRSSYRAGRLYAQAMEFRGEEIPAHLAHLKDTSGGSTAQEASTLLERYGASEDTPVVSFN

Gene
lipA
Protein
Lipoyl synthase
Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Length
348 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.311 kDa
Sequence
MTIAPEGRRLLRVEARNSETPIETKPRWIRNQVKNGPEYQDMKERVAGASLHTVCQEAGCPNIHECWESREATFLIGGANCSRRCDFCMINSARPEPLDRGEPLRVAESVREMQLNYSTITGVTRDDLDDEGAWLYSEVVRKIHELNPHTGVENLVPDFSGKKDLLQEVFESRPEVFAHNVETVPRIFKRIRPAFRYERSLDVIRQARDFGLVTKSNLILGMGETKEEITEALQDLHDAGCDIITITQYLRPGPLFHPIERWVKPEEFLEHADAAKEMGFAAVMSGPLVRSSYRAGRLYAQAMEFRGEEIPAHLAHLKDTSGGSTAQEASTLLERYGASEDTPVVSFN

Gene
lipA
Protein
Lipoyl synthase
Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Length
348 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.384 kDa
Sequence
MTIAPEGRRMLRVEARNSQTPIETKPRWIRNQVKNGPEYKDMKERVAGASLHTVCQEAGCPNIHECWESREATFLIGGANCSRRCDFCMINSARPEPLDRGEPLRVAESVREMRLNYSTITGVTRDDLPDEGAWLYSEVVRKIHELNPNTGVENLVPDFSGKRDLLQEVFESRPEVFAHNLETVPRIFKRIRPAFRYDRSLDVIRQARDFGLVTKSNLILGMGETREEISEALRDLHSAGTDIITITQYLRPGPLFHPIERWVKPEEFLELSDEAYEIGFAAVMSGPLVRSSYRAGKLYAQALKFRGEELPANLSHLAETTEGPTTQEASSLLERYGASEDAPVIPRG

Gene
lipA
Protein
Lipoyl synthase
Organism
Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717)
Length
347 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.087 kDa
Sequence
MAVAPNGRRLLRIEARNAQTPIEAKPRWIRTTATMGPEFRDMKKRVKGAGLHTVCQEAGCPNIHECWEDREATFLIGGDTCSRRCDFCDIKSGRPEPLDEDEPRRVAENVREIGLRYSTITGVTRDDLPDEGAWLYAEVVRQIHKLNPNTGVENLTPDFSGKPDLLQTVFEARPEVFAHNLETVPRIFKRIRPAFRYERSLDVIRQARDFGLVTKSNLILGMGETVDEVKSAMRDLRDAGCDILTVTQYLRPSNLHHPIERWVKPEEFVMYRDYGHDIGFAGVMAGPLVRSSYRAGRLYAQAIKARGEELPANLQHLGEGIDDTASQEASTLLSKYGASRETPVGAR

Gene
lipA
Protein
Lipoyl synthase
Organism
Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109)
Length
347 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.503 kDa
Sequence
MTVSANGRRMLRIEAKNSQTPIEAKPRWIRTTAKMGPEYRDMKNRVTGMSLHTVCQEAGCPNIHECWEDREASFLIGGDTCSRRCDFCQIKSGKPTPLDRDEPRRVAESVREMGLKYATVTGVTRDDLDDEGAWLYAEVVRKIHELNPNTGVENLTPDFSNKPELLQIVFESQPEVFAHNLETVPRIFKRIRPAFKYERSLEVIRAAHDYGLITKSNLILGMGETEEEVVEAMRDLREAGTDILTITQYLRPTSMHHPIERWVRPEEFVAHSEAAYDMGFPAVMSGPLVRSSYRSGRLYAQAMRARGREIPENLSHLNEKLDGSTQQEATNLLDKYGASEETPVAYR

Gene
lipA
Protein
Lipoyl synthase
Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Length
347 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.109 kDa
Sequence
MTNAVQTHMPAARAKPKKAIQGEKLRGYDKVARIPIKIIPTVEAKKKPDWIRVKLSSPAEVARIKSTLREQKLYTVCEEAACPNLPQCFADGTATFMIMGDICTRRCPFCDVGHGRPNELDKDEPRHTAETIQGLGLKYAVITSVDRDDLKDGGAAHFVEVLNESRALSPNCLIEILVPDFRGRMDIALDLLTETAPDVFNHNIETVPRLYKAFRPGSDYQHSLDLLKIYKERRPDIATKCGFMVGLGETEEEIYKLLDDLKAHNVDMITVGQYLQPSKDHAPVDRYVHPDEFQRYMDYGKKIGFFNIWAGPMVRSSYFADRQYYGEDCPAPIRSKKALAAEGKLGC

Gene
lipA
Protein
Lipoyl synthase
Organism
Psychrobacter cryohalolentis (strain K5)
Length
347 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.139 kDa
Sequence
MTNAVQTHTPAARAKPKKAIQGEKLRGYDKVARIPIKIIPTVEAKKKPDWIRVKLSSPAEVARIKSTLREQKLYTVCEEAACPNLPQCFADGTATFMIMGDICTRRCPFCDVGHGRPNELDKDEPRHTAETIQGLGLKYAVITSVDRDDLKDGGAMHFVEVLNESRALSPNCLIEILVPDFRGRMDIALDLLTETAPDVFNHNIETVPRLYKAFRPGSDYQHSLDLLKIYKERRPDIATKCGFMVGLGETEEEIYKLLDDLKAHNVDMITVGQYLQPSKDHAPVDRYVHPDEFQRYMDYGKKIGFFNIWAGPMVRSSYFADRQYYGEDCPAPIRSKKALAAEGKLGC

Gene
lipA
Protein
Lipoyl synthase
Organism
Psychrobacter sp. (strain PRwf-1)
Length
347 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
39.119 kDa
Sequence
MTTTVETFVPEAPPKPKKAIKGEKLRGYDKVARIPIKVIPTVEAPKKPDWIRVKMSSPAEVDRIKKTLRKQKLYTVCEEAACPNLPQCFGDGTATFMIMGDICTRRCPFCDVAHGRPNELDKDEPRHTAETIQGLGLKYAVITSVDRDDLKDGGAQHFVDVINESKALSPNCLIEILVPDFRGRMDVALDLLTETAPDVFNHNIETVPRLYKAFRPGSDYQHSLDLLKQYKARRPDIATKCGFMVGLGETEEEVYALLDDLKAHDVDMITIGQYLQPSKNHAPVDRYVHPDEFQRYMDYGKKIGFFSIWAGPMVRSSYFADRQYYGEDCPAPIRSKKALEAEGKLGC

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas fluorescens (strain SBW25)
Length
341 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
38.187 kDa
Sequence
MTTDAVQTMIPTLDITERPAPAPRAKVEAGVKLRGAEKVARIPVKIIPTTELPKKPDWIRVRIPVSPEVDRIKALLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDVNEPESLAIAIADLKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLSPNVMLETLVPDYRGRMDVALEITAAEPPDVFNHNLETVPRLYKAARPGSDYQWSLTLLQKFKQMMPHIPTKSGLMLGLGETDEEVIEVMKRMREHDIDMLTLGQYLQPSRSHLPVQRFVHPDTFAWFAEEGYKMGFKNVASGPLVRSSYHADEQAKLVKASLVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas fluorescens (strain Pf0-1)
Length
340 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
38.185 kDa
Sequence
MTTDAVQTMIPTLDVTERPAPRPKVEAGVKLRGAEKVARIPVKIIPTTELPKKPDWIRVRIPVSPEVDRIKSLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDVNEPESLAIAIADLKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLSPNVQLETLVPDYRGRMDIALEITAAEPPDVFNHNLETVPRLYKAARPGSDYQWSLTLLQRFKQMMPHIPTKSGLMLGLGETDDEVIEVMKRMREHDIDMLTLGQYLQPSRSHLPVQRFVHPDTFAWFAEEGYKMGFKNVASGPLVRSSYHADEQAKLVKAELLGS

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacterium extorquens (strain CM4 / NCIMB 13688)
Length
339 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.387 kDa
Sequence
MAVVLDLLNKDTRPKLDAPARPRHPEKAHRPDTAIQRKPDWIRVKAPGSKLWAETKDIVRANNLVTVCEEAGCPNIGECWEKRHATFMIMGDTCTRACSFCNVRTGLPAALDEAEPEKVAEAVAKLGLHHVVVTSVDRDDLKDGGAEHFSRTIAAIRRASPGTTVEILTPDFLRKPGALEVVVAAKPDVFNHNMETVPGKYVTVRPGARYFHSVRLLQRVKELDPTIFTKSGIMVGLGEERNEVVQLMDDLRSAEVDFLTIGQYLQPTRKHHEVVRFVPPDEFKAYETTAYAKGFLLVSATPLTRSSHHAGEDFARLKAARLAKLGPAPVAASIRAVNA

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacterium extorquens (strain PA1)
Length
339 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.415 kDa
Sequence
MAVVLDLLNKDTRPKLDAPARPRHPEKAHRPDTAIQRKPDWIRVKAPGSKLWAETKDIVRANNLVTVCEEAGCPNIGECWEKRHATFMIMGDTCTRACSFCNVRTGLPAALDEAEPEKVAEAVAKLGLHHVVVTSVDRDDLKDGGAEHFSRTIVAIRRASPGTTVEILTPDFLRKPGALEVVVAAKPDVFNHNMETVPGKYVTVRPGARYFHSVRLLQRVKELDPTIFTKSGIMVGLGEERNEVVQLMDDLRSAEVDFLTIGQYLQPTRKHHEVVRFVPPDEFKAYETTAYAKGFLLVSATPLTRSSHHAGEDFARLKAARLAKLGPAPVAASIRAVNA

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacterium extorquens (strain CM4 / NCIMB 13688)
Length
339 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.387 kDa
Sequence
MAVVLDLLNKDTRPKLDAPARPRHPEKAHRPDTAIQRKPDWIRVKAPGSKLWAETKDIVRANNLVTVCEEAGCPNIGECWEKRHATFMIMGDTCTRACSFCNVRTGLPAALDEAEPEKVAEAVAKLGLHHVVVTSVDRDDLKDGGAEHFSRTIAAIRRASPGTTVEILTPDFLRKPGALEVVVAAKPDVFNHNMETVPGKYVTVRPGARYFHSVRLLQRVKELDPTIFTKSGIMVGLGEERNEVVQLMDDLRSAEVDFLTIGQYLQPTRKHHEVVRFVPPDEFKAYETTAYAKGFLLVSATPLTRSSHHAGEDFARLKAARLAKLGPAPVAASIRAVNA

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacterium extorquens (strain PA1)
Length
339 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.415 kDa
Sequence
MAVVLDLLNKDTRPKLDAPARPRHPEKAHRPDTAIQRKPDWIRVKAPGSKLWAETKDIVRANNLVTVCEEAGCPNIGECWEKRHATFMIMGDTCTRACSFCNVRTGLPAALDEAEPEKVAEAVAKLGLHHVVVTSVDRDDLKDGGAEHFSRTIVAIRRASPGTTVEILTPDFLRKPGALEVVVAAKPDVFNHNMETVPGKYVTVRPGARYFHSVRLLQRVKELDPTIFTKSGIMVGLGEERNEVVQLMDDLRSAEVDFLTIGQYLQPTRKHHEVVRFVPPDEFKAYETTAYAKGFLLVSATPLTRSSHHAGEDFARLKAARLAKLGPAPVAASIRAVNA

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas entomophila (strain L48)
Length
338 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
38.044 kDa
Sequence
MTTVQEAVPNLIPTQDVTPRPAPKKVEAGVKLRGAEKVARIPVKIIPTEELPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDLDEPKNLAIAIADLRLKYVVITSVDRDDLRDGGAQHFADCIREIRALSPGVQLETLVPDYRGRMDVALEITAQTPPDVFNHNLETVPRLYKAARPGSDYDWSLDLLQKFKQMVPHVPTKSGLMLGLGETDEEVIEVMHRMREHDIDMLTLGQYLQPSRNHLPVQRFVHPDTFAWFAEEGYKMGFKNVASGPLVRSSYHADQQAHEAKIKL

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Length
338 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.957 kDa
Sequence
MTTVQEAVPNLIPTQDATPRPAPKKVEAGVKLRGADKVARIPVKIIPTDELPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDLDEPKNLAVAIADLRLKYVVITSVDRDDLRDGGAQHFADCIREIRALSPGVQLETLVPDYRGRMDVALEITAQEPPDVFNHNLETVPRLYKAARPGSDYDWSLDLLQKFKQLVPHVPTKSGLMLGLGETDEEVIEVMHRMREHDIDMLTLGQYLQPSRSHLPVQRFVHPDTFAWFAEEGYKMGFKNVASGPLVRSSYHADQQAHEAKIKL

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Length
338 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.957 kDa
Sequence
MTTVQEAVPNLIPTQDATPRPAPKKVEAGVKLRGADKVARIPVKIIPTDELPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDLDEPKNLAVAIADLRLKYVVITSVDRDDLRDGGAQHFADCIREIRALSPGVQLETLVPDYRGRMDVALEITAQEPPDVFNHNLETVPRLYKAARPGSDYDWSLDLLQKFKQLVPHVPTKSGLMLGLGETDEEVIEVMHRMREHDIDMLTLGQYLQPSRSHLPVQRFVHPDTFAWFAEEGYKMGFKNVASGPLVRSSYHADQQAHEAKIKL

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas putida (strain W619)
Length
338 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.961 kDa
Sequence
MTTVQEAVPNLIPTQDATPRPAPKKVEAGVKLRGADKVARIPVKIIPTDELPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDVDEPKNLAVAIADLRLKYVVITSVDRDDLRDGGAQHFADCIREIRALSPGVQLETLVPDYRGRMDVALEITAQEPPDVFNHNLETVPRLYKAARPGSDYDWSLDLLQKFKQMVPHVPTKSGLMLGLGETDEEVIEVMHRMREHDIDMLTLGQYLQPSRSHLPVQRFVHPDTFAWFAEEGYKMGFKNVASGPLVRSSYHADQQAHEAKIKL

Gene
lipA
Protein
Lipoyl synthase
Organism
Xanthomonas axonopodis pv. citri (strain 306)
Length
337 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.864 kDa
Sequence
MTQPIARSIPLQVVSGDTAAPAPLQTGVKQIGGDKINRSPVQFVDAPVLRKPSWIRVRIPSGNAVQNLKAKLRENRLVTVCEEASCPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDASEPASLAATVADMGLKYVVVTSVDRDDLRDGGAQHFVDCISAIRTSSPNTRIEILTPDFRGKGRMDRALEILALSPPDVFNHNIETVPDLYPNVRPGADYQWSLTLLQRFKAQHPSIATKSGIMLGLGETMEQVQATLRDLRAHDVDMITIGQYLQPTPHHHPVMRYWTPEEYKALEDYGNALGFSHVASGPMVRSSYHADRQAAGAGVAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Xanthomonas campestris pv. vesicatoria (strain 85-10)
Length
337 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.834 kDa
Sequence
MTQPIARSIPLQVVSGDTAAPAPLQTGVKQIGGDKINRSPVQFVDAPVLRKPSWIRVRIPSGNAVQNLKAKLRENRLVTVCEEASCPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDASEPASLAATVADMGLKYVVVTSVDRDDLRDGGAQHFVDCISAIRASSPNTRIEILTPDFRGKGRMDRALEILALSPPDVFNHNIETVPDLYPNVRPGADYQWSLTLLQRFKAQHPSIATKSGIMLGLGETMEQVQATLRDLRAHDVDMITIGQYLQPTPHHHPVMRYWTPEEYKALEDYGNALGFSHVASGPMVRSSYHADRQAAGAGVAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Xanthomonas campestris pv. campestris (strain 8004)
Length
337 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.896 kDa
Sequence
MTQPIARSIPLQVVSGDTAAPASLQTGVKQIGGDKINRSPVQFVDAPVLRKPSWIRVRIPSGNAVQNLKAKLRENRLVTVCEEASCPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDASEPASLATTVADMGLKYVVVTSVDRDDLRDGGAQHFVDCISAIRASAPKTRIEILTPDFRGKGRMDRALEILATSPPDVFNHNIETVPDLYPNVRPGADYQWSLTLLQRFKAQHPTIATKSGIMLGLGETMEQVQVTLRDLRAHDVDMITIGQYLQPTPHHHPVMRYWTPEEYKALEEYGNALGFSHVASGPMVRSSYHADRQAAGAGVAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Xanthomonas campestris pv. campestris (strain B100)
Length
337 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.884 kDa
Sequence
MTQPIARSIPLQVVSGDTAAPASLQTGVKQIGGDKINRSPVQFVDAPVLRKPSWIRVRIPSGNAVQNLKAKLRENRLVTVCEEASCPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDASEPTSLATTVADMGLKYVVVTSVDRDDLRDGGAQHFVDCISAIRASAPKTRIEILTPDFRGKGRMDRALEILATSPPDVFNHNIETVPDLYPNVRPGADYQWSLTLLQRFKAQHPTIATKSGIMLGLGETMEQVQATLRDLRAHDVDMITIGQYLQPTPHHHPVMRYWTPEEYKALEDYGNALGFSHVASGPMVRSSYHADRQAAGAGVAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Length
337 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.896 kDa
Sequence
MTQPIARSIPLQVVSGDTAAPASLQTGVKQIGGDKINRSPVQFVDAPVLRKPSWIRVRIPSGNAVQNLKAKLRENRLVTVCEEASCPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDASEPASLATTVADMGLKYVVVTSVDRDDLRDGGAQHFVDCISAIRASAPKTRIEILTPDFRGKGRMDRALEILATSPPDVFNHNIETVPDLYPNVRPGADYQWSLTLLQRFKAQHPTIATKSGIMLGLGETMEQVQVTLRDLRAHDVDMITIGQYLQPTPHHHPVMRYWTPEEYKALEEYGNALGFSHVASGPMVRSSYHADRQAAGAGVAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Length
337 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.944 kDa
Sequence
MTQPTARSIPLQVVSGDTAAPAPLQTGVKQIGGDKIHRSPVQFVDAPVLRKPSWIRVRIPSGNAVQNLKAKLRENRLVTVCEEASCPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDANEPASLAITVADMGLKYVVVTSVDRDDLRDGGAQHFVDCISAIRTSSPNTRIEILTPDFRGKGRMDRALDILALSPPDVFNHNIETVPDLYPNVRPGADYQWSLTLLQRFKAQHPSIATKSGIMLGLGETMEQVQATLRDLRAHDVDMITIGQYLQPTPHHHPVMRYWTPEEYKALEEYGNALGFSHVASGPMVRSSYHADRQAAGAGVAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Length
337 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.944 kDa
Sequence
MTQPTARSIPLQVVSGDTAAPAPLQTGVKQIGGDKIHRSPVQFVDAPVLRKPSWIRVRIPSGNAVQNLKAKLRENRLVTVCEEASCPNIHECFSHGTATFMILGEVCTRRCSFCDVAHGRPKPPDANEPASLAITVADMGLKYVVVTSVDRDDLRDGGAQHFVDCISAIRTSSPNTRIEILTPDFRGKGRMDRALDILALSPPDVFNHNIETVPDLYPNVRPGADYQWSLTLLQRFKAQHPSIATKSGIMLGLGETMEQVQATLRDLRAHDVDMITIGQYLQPTPHHHPVMRYWTPEEYKALEEYGNALGFSHVASGPMVRSSYHADRQAAGAGVAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Stenotrophomonas maltophilia (strain R551-3)
Length
336 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.062 kDa
Sequence
MTESTARSIPLQIVQGDSPSAAPLQAGVKQLGGDKINRSPVQFADAPVLRKPSWIRVRIPSGNAVQNLKAKLRENRLVTVCEEASCPNIHECFGHGTATFMILGEVCTRRCSFCDVAHGRPKPPDANEPASLGQTVADMGLKYVVVTSVDRDDLRDGGAQHFVDCISAIREKSPGTRIEVLTPDFRGKGRMERALEILAQNPPDVFNHNIETVPDLYRNVRPGADYQWSLNLLKNFKAQHPEVPTKSGIMLGLGEEFEQIKATMRDLRAHDVDMITIGQYLQPTAHHHPVLKYWTPEDYKALEDYGYELGFSHVASGPMVRSSYHADVQAKGAGVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Stenotrophomonas maltophilia (strain K279a)
Length
336 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.044 kDa
Sequence
MTETTARSIPLQIVQGDSPSAAPLQAGVKQLGGDKINRSPVQFADAPVLRKPSWIRVRIPSGNAVQNLKAKLRENRLVTVCEEASCPNIHECFGHGTATFMILGEVCTRRCSFCDVAHGRPKPPDANEPASLGQTVADMGLKYVVVTSVDRDDLRDGGAQHFVDCITAIREKSPGTRIEVLTPDFRGKGRMERALEILAQNPPDVFNHNIETVPDLYRNVRPGADYQWSLNLLKNFKAQHPDVPTKSGIMLGLGEDFEQIKATLRDLRAHDVDMITIGQYLQPTAHHHPVLKYWTPEDYKALEDYGYELGFSHVASGPMVRSSYHADVQAKGAGVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201)
Length
335 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.98 kDa
Sequence
MTIAPEGRKLLRVEARNAEVPIEKKPSWLKNTAKMGPQFTELKSMARGRGLHTVCEEAGCPNIYECWEDREATFLIGGDTCTRRCDFCDIATGKPGMVDVAEPRKVAESVRDLGLRYATVTSVARDDLADGGAWLNAETIRAIHAMNPSTGVEILIPDFKGQPDAVQQVIDAQPEVFAHNLETVPRIFKQIRPAFAYERSLDVLTQGKEHGMIVKSNLILGMGETDDEVYEALCDLHDAGCDIITLTQYLRPGPTFHPIDRWVKPETFVELSKAAEEIGFLGVMAGPMVRSSYRAGKLWARAMKKMGREIPEHLSHIDDSGSATQEASSLLARLG

Gene
lipA
Protein
Lipoyl synthase
Organism
Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230)
Length
335 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.637 kDa
Sequence
MSLAPEGRRLLRVEARNAEVPVERKPEWIKAKVHMGPEYIGLKNKVKSAGLHTVCEEAGCPNIFECWEDREATFLIGGDICTRRCDFCDITSGKPRPLDMEEPQKVAENIREMDLRYATVTGVARDDQKDGAAWLYAETIRRIHALNPGTGVEILPPDFGAVPELVQQVFDARPEVFAHNLETVPRIFKRIRPAFTYEKSLRVLTMAKADGLVTKSNLILGMGEEDHEIDQALVDLHESGCDIITITQYVRPSKLHHPIDRWVKPQEFVQWSQRAEEIGFQGVMAGPLVRSSYRAGKLYAQAMQRLGRTLPENLAHLAGEKTARQEASAVVAQMS

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
Length
335 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.665 kDa
Sequence
MTDTVQTLIPTLDVSERVARPKVEAGVKLRGAEKVARIPVKIIPTVDLPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDVNEPKSLAIAIADLRLKYVVITSVDRDDLRDGGAQHFADCIREIRLLSPGVQLETLVPDYRGRMDVALEITAAEPPDVFNHNLETVPRLYKAARPGSDYQWSLTLLQRFKQMVPHVPTKSGLMLGLGETDEEVIEVMQRMREHDIDMLTLGQYLQPSRNHLPVQRFVHPDTFAWFAEEGYKMGFKNVASGPLVRSSYHADEQAKIAKAML

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas syringae pv. syringae (strain B728a)
Length
335 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.665 kDa
Sequence
MTDTVQTLIPTLDVSERVARPKVEAGVKLRGAEKVARIPVKIIPTVDLPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDVNEPKSLAIAIADLRLKYVVITSVDRDDLRDGGAQHFADCIREIRLLSPGVQLETLVPDYRGRMDVALEITAAEPPDVFNHNLETVPRLYKAARPGSDYQWSLTLLQRFKQMVPHVPTKSGLMLGLGETDEEVIEVMQRMREHDIDMLTLGQYLQPSRNHLPVQRFVHPDTFAWFAEEGYKMGFKNVASGPLVRSSYHADEQAKIAKAML

Gene
lipA
Protein
Lipoyl synthase
Organism
Herminiimonas arsenicoxydans
Length
335 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.333 kDa
Sequence
MTIDTNPESSTPSAPAYNPSEKQKGSAKTIRIPIKVVPMERLPKPDWIRVKAGSPSTRFYEIKDILRANNLVTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPENLAKTIAALRLNYVVITSVDRDDLRDGGAGHFAECIRRVRELSPNTRIEILVPDFRGRMDRALEILNLAPPDVMNHNLETAPRLYKEARPGSDYAYSLNLLKRFKALHPNTPTKSGIMVGLGETDEEVLQVMRDMRAHDVDMLTIGQYLMPSGDHLPVRRYVHPDTFKMYEEEAYKMGFAHAAVGAMVRSSYHADQQAHGVTAGASQLPHD

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
Length
334 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.842 kDa
Sequence
MAVVLDLLNNDTRPKVEAPARPRHPEKAHRPDTAIQRKPDWIRVKAPGSKLWAETKDIVRANNLVTVCEEAGCPNIGECWEKRHATFMIMGDTCTRACAFCNVRTGLPESLDAAEPEKVADAVAKLGLHHVVVTSVDRDDLKDGGAEHFSRTIAAIRRASPGTTVEILTPDFLRKPGALEVVVAAKPDVFNHNLETVPGKYVTVRPGARYFHSVRLLQRVKELDPTIFTKSGIMVGLGEERNEVVQLMDDLRSAEVDFLTIGQYLQPTRKHHEVVRFVPPDEFKAYETTAYAKGFLLVSATPLTRSSHHAGEDFARLKAARLAKLGPAPVAVNA

Gene
lipA
Protein
Lipoyl synthase
Organism
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1)
Length
334 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.271 kDa
Sequence
MSDALIAPNASSSEAPQSPAEHYDPTRKQKSADKTARIPIKIVPAEKLKKPDWIRVKAATGNSRFYEIKDILRANNLVTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPGNLARTIAQLKLNYVVITSVDRDDLRDGGAQHYVDCISQTRELSPATRIEVLVPDFRGRLDKALDILQACPPDVMNHNMETVPRLYKQARPGADYAHSLKLLQEFKRRNPNVPTKSGLMVGLGETDEEILEVMRDMRAHDIDMLTIGQYLAPSNHHLPVLRYVHPDTFKMFEEEAYKMGFTHAAVGAMVRSSYHADQQAHQAGFA

Gene
lipA
Protein
Lipoyl synthase
Organism
Halorhodospira halophila (strain DSM 244 / SL1)
Length
334 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.704 kDa
Sequence
MSEFKGIPVSSGSVVERDGVRTIKDGVKRRDDGQGAVRRRKPQWLKARAPGGEGYRSVRGIVHDHHLSTVCEESHCPNLGECWSHGTATFMVLGSVCTRTCRFCSVDTGNPKGRLDPQEPEHCAESVRLMGLRYVVLTSVDRDDLPDGGAEHYAQCVRAIKADNPDTAVEALTPDFRGDEEAVRTVVDSGLEVFAHNVEVVRRLSPQVRDPRAGYEQSLAVLQVAKRLRPGVLTKSSLMVGLGETDAEIDEAFDDLLRAEVDIVTLGQYLQPTRNHLPVERFVSPDEFEALRQEGLRRGFREVVAGPLVRSSYRADRVLEGNNVGLPSVGPDVG

Gene
lipA
Protein
Lipoyl synthase
Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
Length
333 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.103 kDa
Sequence
MSTLVESPVPSNDSQAAAPAAYDPTQKQKSQAKTARIPIKVVAAEKLKKPEWIRVRAAAPGSRFYDIKRILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDTQEPENLARTIAALKLSYVVITSVDRDDLRDGGAAHFVECIAKVREYSPDTRIEVLVPDFRGRLDRALHILNSGPPDVMNHNLETVPRLYKQARPGSDYAHSLKLLAEFKKLHPEVPTKSGLMLGLGETDEEILQVMRDMREHNVDMLTIGQYLQPSEHHLPVLRYVHPDTFAMFEREAYAMGFTHAAVGAMVRSSYHADQQAHAAGVN

Gene
lipA
Protein
Lipoyl synthase
Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Length
333 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.131 kDa
Sequence
MSTLVESPVPSNDSQAAAPAAYDPTQKQKSQAKTARIPIKVVAAEKLKKPEWIRVRAAAPGSRFYDIKRILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDTQEPENLARTIAALKLSYVVITSVDRDDLRDGGAAHFVECIAKVREYSPDTRIEVLVPDFRGRLDRALHILNSGPPDVMNHNLETVPRLYKQARPGSDYAHSLKLLVEFKKLHPEVPTKSGLMLGLGETDEEILQVMRDMREHNVDMLTIGQYLQPSEHHLPVLRYVHPDTFAMFEREAYAMGFTHAAVGAMVRSSYHADQQAHAAGVN

Gene
lipA
Protein
Lipoyl synthase
Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Length
333 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.103 kDa
Sequence
MSTLVESPVPSNDSQAAAPAAYDPTQKQKSQAKTARIPIKVVAAEKLKKPEWIRVRAAAPGSRFYDIKRILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDTQEPENLARTIAALKLSYVVITSVDRDDLRDGGAAHFVECIAKVREYSPDTRIEVLVPDFRGRLDRALHILNSGPPDVMNHNLETVPRLYKQARPGSDYAHSLKLLAEFKKLHPEVPTKSGLMLGLGETDEEILQVMRDMREHNVDMLTIGQYLQPSEHHLPVLRYVHPDTFAMFEREAYAMGFTHAAVGAMVRSSYHADQQAHAAGVN

Gene
lipA
Protein
Lipoyl synthase
Organism
Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216)
Length
333 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.885 kDa
Sequence
MTIAPEGRRMLRIEARNAETPIERKPSWIRTKARTGPDYTELKGLVKSGGLHTVCEEAGCPNIYECWEDREATFLIGGSECTRRCDFCQIDTGKPSPLDRDEPRRVAESIATMGLRYATITGVARDDLDDGGAWLYAETIRATHAANPGTGVEILVPDFNGKPELLQQVFDAQPEVFAHNVETVPRIFKSIRPAFRYERSLDVITQGRDAGLVTKSNLILGMGETDEEVLEALADLRGAGCDIITITQYLRPTPRHHPVERWVKPEKFVEFSAEAERLGFAGVMAGPLVRSSYRAGRLWAQAMKRRGVAIPAQLAHLDKESPAAQEASSLLAR

Gene
lipA
Protein
Lipoyl synthase
Organism
Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
Length
333 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.305 kDa
Sequence
MTAAPEGRKLLRLEVRNSQTPIEKKPSWIKTRARMGPEYQELKGLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDVEEPRRVAESVQAMGLRYSTVTGVARDDLEDGGAWLYAETVRQIHQLNPGTGVELLIPDFNADPGQLAEVFGSRPEVLAHNVETVPRIFKRIRPAFRYERSLEVITRAREDGLVTKSNLILGMGETPEEVTEALRDLREAGTDIITITQYLRPSPRHHPVERWVKPEEFVEHTRTAEELGFPGVMAGPLVRSSYRAGRLYAKATEHRGMPLPDNLAHLAKAGTAAQEASSLLSR

Gene
lipA
Protein
Lipoyl synthase
Organism
Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3)
Length
333 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.294 kDa
Sequence
MTAVAPEGRPLLRIEARNAQTPIERKPSWIRTRLRTGPQYQDVKGLVQSAGLHTVCEEAGCPNIYECWEDREATFLIGGEVCTRRCDFCQIDSGRPAPLDHDEPRRVAESVATMGLRYATVTGVARDDLADGGSWLYAETVRQIHARSADTGVEVLIPDFGGRPDQLGEVFEAAPEVLAHNLETVPRIFRRIRPAFRYERSLDVLRQARQAGLVTKSNLILGLGETAEEIHTALRDLRSAGCELLTVTQYLRPTPRHHPVERWVRPEEFLDWGRVGAELGFSGVMSGPLVRSSYRASRLYQQAMTARDQDRSEMSVPPESVSENSHGQRPSPW

Gene
lipA
Protein
Lipoyl synthase
Organism
Ralstonia pickettii (strain 12J)
Length
333 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.988 kDa
Sequence
MTDSAAGATEVATPATPSNKPYDATAKQKSLDKTARIPIKIVPAEKLKKPDWIRVRAATGNSRFYEIKDILRANNLVTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPENLAKTIAELKLNYVVITSVDRDDLRDGGAQHYVDCISRTRALSPATRIEVLVPDFRGRLEKALDILQECPPDVMNHNLETVPRLYKQARPGADYAHSLKLLKDFKARNPNVPTKSGLMVGLGETDEEILEVMRDMREHDIDMLTIGQYLAPSGHHLPVLRYVHPDTFKMFEEKAYEMGFTHAAVGAMVRSSYHADQQAHEAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Ralstonia solanacearum (strain GMI1000)
Length
333 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.084 kDa
Sequence
MTDSASGASAVANIATPSNEPYDATRKQKSLDKTARIPIKIVPAEKLKKPEWIRVKAATGNSRFYEIKDILRANNLVTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDANEPENLAKTIAQLRLNYVVITSVDRDDLRDGGAQHYVDCISRTRELSPATRIEVLVPDFRGRLEKALDILQACPPDVMNHNMETVPRLYKQARPGADYAHSLKLLKDFKARNPNLPTKSGLMVGLGETDEEILEVMRDMREHDIDMLTIGQYLAPSGHHLPVLRYVHPDTFKMFEEKAYEMGFTHAAVGAMVRSSYHADQQAHEAGFA

Gene
lipA
Protein
Lipoyl synthase
Organism
Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
Length
332 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.752 kDa
Sequence
MTIAPEGRRLLRVEARNAAVPIEKKPPWIKTRATMGPEYTELRSLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPADFDADEPRRVAESVQAMGLRYSTVTGVARDDLADGGAWLYAETVRQIHALNPGTGVELLIPDFNAEPDQLAEVFSSRPEVLAHNLETVPRVFKRIRPGFRYARSLSVLTAARDAGLVTKSNLILGMGETTAEAVEALADLHAAGCDLVTITQYLRPSPRHHPVERWVKPEEFVELSDEAERIGFLGVMAGPLVRSSYRAGRLWGQAMARRGLEVPPALAHLTEPTTSRQEAASLLR

Gene
lipA
Protein
Lipoyl synthase
Organism
Verminephrobacter eiseniae (strain EF01-2)
Length
332 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.023 kDa
Sequence
MASADRQMIGDATLAYDPRAKQKAAAKLARIPIKVEPGERLKKPDWIRVKAASPGTRFDDIKRILREHRLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDQDEPMNLARTVAALALEYVVITSVDRDDLRDGGSGHFVDCIQSIRKLSPQTRIEILVPDFRGRDDRALAILQAAPPDVMNHNLETAPRLYPQARPGSDYRFSLNLLKKFKALHPTVPTKSGIMVGLGETDEEILQVMRDMRAHGIEMLTIGQYLAPSSSHLPVRRYVHPDDFRMFEQEAYRMGFSHAAVGAMVRSSYHADRQAQAAGLHVNAPK

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidovorax citrulli (strain AAC00-1)
Length
332 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.947 kDa
Sequence
MSTPEVVREAQSTVAYNPLAKQKAAAKLSRIPIKVEQGEVLKKPEWIRVKAGSPTTRFYEIKEILREHKLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDKDEPLNLARTIAALKLKYVVITSVDRDDLRDGGSGHFVECIQNIRALSPATQIEILVPDFRGRDDRALEILKAAPPDVMNHNLETAPRLYKEARPGSDYQFSLNLLKKFKALHPGVPTKSGIMVGLGETDEEILQVMRDMRAHDIDMLTIGQYLAPSNSHLPVRRYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADQQAHAAGLQAGPQG

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidovorax citrulli (strain AAC00-1)
Length
332 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.947 kDa
Sequence
MSTPEVVREAQSTVAYNPLAKQKAAAKLSRIPIKVEQGEVLKKPEWIRVKAGSPTTRFYEIKEILREHKLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDKDEPLNLARTIAALKLKYVVITSVDRDDLRDGGSGHFVECIQNIRALSPATQIEILVPDFRGRDDRALEILKAAPPDVMNHNLETAPRLYKEARPGSDYQFSLNLLKKFKALHPGVPTKSGIMVGLGETDEEILQVMRDMRAHDIDMLTIGQYLAPSNSHLPVRRYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADQQAHAAGLQAGPQG

Gene
lipA
Protein
Lipoyl synthase
Organism
Polaromonas naphthalenivorans (strain CJ2)
Length
332 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.023 kDa
Sequence
MSTPEVVREVQSLETYNPLAKQKAAAKLSRIPVKVVQGEILKKPDWIRVKAGSPSTRFYEIKQILRENKLNTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPLNLARTIAALKLKYVVITSVDRDDLRDGGSGHFVECIQRIRELSPGTTIEVLVPDFRGRDDRALEILKTSPPDVMNHNLETAPRLYKEARPGSDYQFSLNLLKKFKALHPDVPTKSGIMVGLGETDEEILQVMQDMRDHGINMLTIGQYLAPSTSHLPVRRYVHPDTFKMFEEKAYEMGFSHAAVGAMVRSSYHADQQAHAAGVSDKPAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Hahella chejuensis (strain KCTC 2396)
Length
332 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.965 kDa
Sequence
MSETNVQGSLAEAPKAAVKRVEQGVKLRGYDKVSRNPVKIIATDAVPRKPDWIRVRLSSSPSVEAIKQKLRKLNLHSVCEEASCPNLSECFSHGTATFMIMGDICTRRCPFCDVAHGRPNALDENEPTHLAQAIAEMNLKYVVITSVDRDDLRDGGAGHFAKCISESRKYSPNLKIEVLVPDFRGRMDVALDILRESPPDVFNHNLETVPRLYKQARPGADYAWSLLLLKRFKEAAPDVPTKSGLMLGIGEEIEEVKQVMRDLRAHNTDMLTLGQYLAPSKDHLPVVRFVHPDEFKELADYGYEIGFKQVASGPLVRSSYHADKQAAGETIS

Gene
lipA
Protein
Lipoyl synthase
Organism
Bordetella avium (strain 197N)
Length
331 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.799 kDa
Sequence
MSTQLDASQPSNDVASPAAYDPTQKQKSQAKTARIPIKVIPAERLKKPEWIRVRAAAPGSRFYDIKRILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDAQEPENLARTIAALKLSYVVITSVDRDDLRDGGAAHFVECITKIRELSPITRIEVLVPDFRGRLDRALAILNAGPPDVMNHNLETVPRLYKQARPGSDYLHSLKLLAEFKALHPDVPTKSGLMLGLGETDEEILEVMRDMRAHNVDMITIGQYLQPSEHHLPVLRYVHPDTFAMFEREAYAMGFSHAAVGAMVRSSYHADEQAHAAGVN

Gene
lipA
Protein
Lipoyl synthase
Organism
Janthinobacterium sp. (strain Marseille)
Length
331 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.041 kDa
Sequence
MTTETNPAVTPAYNPSEKQKGAAKTIRIPIKVIPMERLPKPDWIRVKAASPSTRFYEIKDILRANNLVTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPENLAKTIAALRLNYVVITSVDRDDLRDGGAGHFAECIRRVRELSPNTRIEILVPDFRGRMDRALEILNAAPPDVMNHNLETAPRLYKEARPGSDYEYSLNLLKRFKAQHPNTPTKSGIMVGLGETDEEVLQVMRDMRAHDVDMLTIGQYLMPSGDHLPVRRYVHPDTFKMYEEEAYKMGFAHAAVGAMVRSSYHADQQAHGVTSAQSDVVNK

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6)
Length
331 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.783 kDa
Sequence
MSTENTTRQAETGAAYDATAKQKAQAKTARIPIKVVPAETLKKPDWIRVKAGSPTTRFYEIKNILREHQLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPANLAKTIAALKLKYVVITSVDRDDLRDGGAGHYVECIRQTRAASPETRIEVLVPDFRGRMDRALEILKTAPPDVMNHNMETVPRLYKEARPGADYQFSLTLLKRFKEEVPGVPTKSGLMVGLGETDDEILDVMRDMRAHDIDMLTIGQYLAPSGHHLPVRRYVHPDTFRMFETEAYKMGFTHAAVGAMVRSSYHADQQAHQAGVDGAIG

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6)
Length
331 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.783 kDa
Sequence
MSTENTTRQAETGAAYDATAKQKAQAKTARIPIKVVPAETLKKPDWIRVKAGSPTTRFYEIKNILREHQLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPANLAKTIAALKLKYVVITSVDRDDLRDGGAGHYVECIRQTRAASPETRIEVLVPDFRGRMDRALEILKTAPPDVMNHNMETVPRLYKEARPGADYQFSLTLLKRFKEEVPGVPTKSGLMVGLGETDDEILDVMRDMRAHDIDMLTIGQYLAPSGHHLPVRRYVHPDTFRMFETEAYKMGFTHAAVGAMVRSSYHADQQAHQAGVDGAIG

Gene
lipA
Protein
Lipoyl synthase
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Length
331 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.024 kDa
Sequence
MSDALIATSSEAPQSPAEQYDPTRKQKSADKTARIPIKIVPAEKLKKPDWIRVKAATGSSRFYEIKDILRANNLVTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPGNLARTIAQLKLNYVVITSVDRDDLRDGGAQHYVDCISQTRELSPATRIEVLVPDFRGRLDKALDILQACPPDVMNHNMETVPRLYKQARPGADYEHSLKLLQEFKRRNPNVPTKSGLMVGLGETDEEILEVMRDMRAHDIDMLTIGQYLAPSNHHLPVLRYVHPDTFKMFEEEAYKMGFTHAAVGAMVRSSYHADQQAHQAGFA

Gene
lipA
Protein
Lipoyl synthase
Organism
Cupriavidus necator (strain JMP 134 / LMG 1197)
Length
331 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.979 kDa
Sequence
MSDALIASSSEAPQSPAEQYDPTRKQKSADKTARIPIKIVPAEKLKKPDWIRVKAATGNSRFYEIKDILRANNLVTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPGNLARTIAQLKLNYVVITSVDRDDLRDGGAQHYVDCISQTRELSPATRIEVLVPDFRGRLDKALDILQACPPDVMNHNMETVPRLYKQARPGADYAHSLKLLQEFKRRNPNVPTKSGLMVGLGETDEEILEVMRDMRAHDIDMLTIGQYLAPSNHHLPVLRYVHPDTFKMFEEEAYKMGFTHAAVGAMVRSSYHADQQAHQAGFA

Gene
lipA
Protein
Lipoyl synthase
Organism
Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382)
Length
331 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.8 kDa
Sequence
MTAATAPDGRRMLRLEVRNAETPIERKPGWIKTTARMGPEYQALQQLVKTEDLHTVCQEAACPNIYECWEDREATFLIGGSQCTRRCDFCQIDTGKPADYDTDEPRRVADSVRRMGLRYATVTGVARDDLPDEGAWLHAETVRRIHADNPGTGVEILATDFSGNPDLLAEVFSSRPEVFAHNVETVPRIFKRIRPAFRYERSLDVITQARDAGLITKSNLILGMGETRDEVSEALVDLHDAGCDIITVTQYLRPSPRHLPVARWVRPEEFVEIKAEAEAIGFLGVLAGPLVRSSYRAGRLYAQSMRAKGRELPEGLAHLADPANGFAQAVG

Gene
lipA
Protein
Lipoyl synthase
Organism
Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1)
Length
331 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.573 kDa
Sequence
MPTLKGIPVVTSGMKVERDGVRAIKDGVKHNPRAEAAPRGRKPSWLRARVPSGEGYQAVRDIVRTHRLSTVCEESHCPNIGECWNAGTATIMLMGAVCTRACRFCAVDTGNPKGRLDHDEPAHAADSVRLMGLSYVVLTSVDRDDLEDGGAGHYAACVNAIREVNPETAVEVLTPDFNGVPEHVHRVVDARPEVFAQNVETVRRLTHPVRDPRAGYEQTLEVLRLAKARRPDMLTKTSLMLGLGERDEEIRETLEDLRAVGVDIVTFGQYLQPTRNHLPVERYVSPAEFADYRRMGLEMGFLEVVAGPMVRSSYRADKVLEKNNVGLESAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Length
331 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.037 kDa
Sequence
MTQQDPSTKEPKFIKNGIYRKDSVPVREKKPEWLKVTIPTGQVFTEVRKIVKEHRLHTVCEEAMCPNIGECWSRGTATFMLMGHICTRACRFCAVDTGNPMGKLDLDEPRSVADSVRLMDLKYVVLTSVDRDDLPDGGAYHFAKTVKAIKEVNPQTRVEALTPDFGGNTACVDLVLDSGVDTYAQNLETVRRLTHPVRDIRASYDRTLSVLAHAKQARPDVITKTSLMLGLGETREEIREAMADCRAAGVDVLTFGQYLRPTMHHLPVERYISPAEFDEIREEGMQLGFLEVVSGPLVRSSYKAEQIVMDRPGNLPEHLSHLDGGSELTLI

Gene
lipA
Protein
Lipoyl synthase
Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Length
330 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.442 kDa
Sequence
MTTATGTKPKKMEAFKMERGVKYRDAAKTSVIQVRNIDPDQELLPKPSWMKIKLPAASAKIDSIKHGMRRHGLHSVCEEASCPNLHECFNHGTATFMIMGAICTRRCPFCDVAHGKPLPLDPEEPRKVAETVQDMKLKYVVITSVDRDDLADRGAAHFAATVREIKALNPECKVEILVPDFRGRVEQAVEILKQNPPDVFNHNLENVPRLYREVRPGADYKWSLELLKIFKQEFPNIPTKSGLMVGLGETNEEILEVMQDLRDHGVTMLTIGQYLQPSRHHLKVERYVPPEEFDMFRSEAERMGFEHAACGPFVRSSYHADLQAKGELVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
Length
330 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.442 kDa
Sequence
MTTATGTKPKKMEAFKMERGVKYRDAAKTSVIQVRNIDPDQELLPKPSWMKIKLPAASAKIDSIKHGMRRHGLHSVCEEASCPNLHECFNHGTATFMIMGAICTRRCPFCDVAHGKPLPLDPEEPRKVAETVQDMKLKYVVITSVDRDDLADRGAAHFAATVREIKALNPECKVEILVPDFRGRVEQAVEILKQNPPDVFNHNLENVPRLYREVRPGADYKWSLELLKIFKQEFPNIPTKSGLMVGLGETNEEILEVMQDLRDHGVTMLTIGQYLQPSRHHLKVERYVPPEEFDMFRSEAERMGFEHAACGPFVRSSYHADLQAKGELVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Length
330 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.442 kDa
Sequence
MTTATGTKPKKMEAFKMERGVKYRDAAKTSVIQVRNIDPDQELLPKPSWMKIKLPAASAKIDSIKHGMRRHGLHSVCEEASCPNLHECFNHGTATFMIMGAICTRRCPFCDVAHGKPLPLDPEEPRKVAETVQDMKLKYVVITSVDRDDLADRGAAHFAATVREIKALNPECKVEILVPDFRGRVEQAVEILKQNPPDVFNHNLENVPRLYREVRPGADYKWSLELLKIFKQEFPNIPTKSGLMVGLGETNEEILEVMQDLRDHGVTMLTIGQYLQPSRHHLKVERYVPPEEFDMFRSEAERMGFEHAACGPFVRSSYHADLQAKGELVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
Length
330 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.442 kDa
Sequence
MTTATGTKPKKMEAFKMERGVKYRDAAKTSVIQVRNIDPDQELLPKPSWMKIKLPAASAKIDSIKHGMRRHGLHSVCEEASCPNLHECFNHGTATFMIMGAICTRRCPFCDVAHGKPLPLDPEEPRKVAETVQDMKLKYVVITSVDRDDLADRGAAHFAATVREIKALNPECKVEILVPDFRGRVEQAVEILKQNPPDVFNHNLENVPRLYREVRPGADYKWSLELLKIFKQEFPNIPTKSGLMVGLGETNEEILEVMQDLRDHGVTMLTIGQYLQPSRHHLKVERYVPPEEFDMFRSEAERMGFEHAACGPFVRSSYHADLQAKGELVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
Length
330 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.884 kDa
Sequence
MSDAPIATSSEVTQSPADYDPTKKQKSAEKTARIPIKIVPAEKLKKPDWIRVKAATGNSRFYEIKDILRANNLVTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPGNLARTIAQLKLNYVVITSVDRDDLRDGGAQHYVDCISQTRELSPNTRIEVLVPDFRGRLDRALDILQACPPDVMNHNMETVPRLYKQARPGADYAHSLKLLQDFKRRNPNVPTKSGLMVGLGETDEEILDVMRDMRAHDIDMLTIGQYLAPSNHHLPVTRYVHPDTFKMFEEEAYKMGFTHAAVGAMVRSSYHADQQAHQAGFA

Gene
lipA
Protein
Lipoyl synthase
Organism
Cutibacterium acnes (strain DSM 16379 / KPA171202)
Length
330 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.521 kDa
Sequence
MSVEADGRKLLRVEVKNSQTPIENKPHWIKTRATMGPEYRDMRRRMIDGDLHTVCQEAGCPNIFECWEDREATFLIGGDHCTRRCDFCQIESAKPEGYDKDEPRRVAESVKQMGLRYATVTSVCRDDLEDEGAWLCAETIRQIHQVTPGVGVEMLAQDFSGKQDLLDIVFEARPEVFGHNLETVPRIFKRIRPGFRYDRSLAVLDSAHEAGLITKSNLILGMGETREEISQAMRALHDANTDLLTITQYLRPNSYLHPIDRWVTPQEFDELAEEAREIGFVGVMSGPLVRSSYRAGRLYRQAMEARGERPVMIVTGYRDGAKPAPFAAKE

Gene
lipA
Protein
Lipoyl synthase
Organism
Actinobacillus pleuropneumoniae serotype 3 (strain JL03)
Length
330 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.458 kDa
Sequence
MTTATGTKPKKMEAFKMERGVKYRDAAKTSVIQVRNIDPDQELLPKPSWMKIKLPAASAKIDSIKHGMRRHGLHSVCEEASCPNLHECFNHGTATFMIMGAICTRRCPFCDVAHGKPLPLDLEEPRKVAETVQDMKLKYVVITSVDRDDLADRGAAHFAATVREIKALNPECKVEILVPDFRGRVEQAVEILKQNPPDVFNHNLENVPRLYREVRPGADYKWSLELLKIFKQEFPNIPTKSGLMVGLGETNEEILEVMQDLRDHGVTMLTIGQYLQPSRHHLKVERYVPPEEFDMFRSEAERMGFEHAACGPFVRSSYHADLQAKGELVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Length
330 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.512 kDa
Sequence
MTTAIGKKTTKLEPFKMERGVKYRDAAKTSVIQVRNIDPDQELLKKPEWMKIKLPTNSAKIDSIKYGMRRHGLHSVCEEASCPNLHECFNHGTATFMIMGAICTRRCPFCDVAHGKPLPLDPYEPRKVAETVQDMKLKYVVITSVDRDDLADRGAAHFAATVREIKALNPECKVEILVPDFRGRVEQAVAILKQNPPDVFNHNLENVPRLYREIRPGADYKWSLELLKIFKQEFPNIPTKSGLMVGLGETNEEILAVMQDLRDHGVTMLTVGQYLQPSRHHLRVERYVPPAEFEMFRSEAEKMGFEHAACGPFVRSSYHADLQAKGELVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Legionella pneumophila (strain Paris)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.742 kDa
Sequence
MGKLIDIPIVVESGQKYKTSQGVTAIKDGIKSSGQDHERLPKPKWLRIVNHTTPAYSQVKEQVQKHRLATVCEEAKCPNISECWSHGTATIMLMGAVCTRACRFCSVDTGNPHGWLDAEEPENTAETVALMNLDYVVLTSVNRDDLPDGGANHYAKTIRAIKKRSPRTKVEALTPDFQGSERDVAVLLDSGVDVFAQNVETVERLTHPVRDNRAGYQQTLNVLAFAKKYRPDVLTKTSLMLGLGETDEEIIQTMDDLRTHHVDILTLGQYLQPTKNHLPIARYVTPETFSELRQIGLKKGFFEVASGPLVRSSYRADRVFKRDNLGLDV

Gene
lipA
Protein
Lipoyl synthase
Organism
Legionella pneumophila (strain Corby)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.77 kDa
Sequence
MGKLIDIPIVVESGQKYKTSQGVTAIKDGIKSSGQDHERLPKPKWLRIVNHTTPAYSQVKEQVQKHRLATVCEEAKCPNISECWSHGTATIMLMGAVCTRACRFCSVDTGNPHGWLDAEEPENTAETVALMNLDYVVLTSVNRDDLPDGGANHYAKTIRAIKKRSPRTKVEALTPDFQGSERDVAVLLDSGVDVFAQNVETVERLTHPVRDNRAGYQQTLNVLAFAKKYRPDVLTKTSLMLGLGETDEEIIRTMDDLRTHHVDILTLGQYLQPTKNHLPIARYVTPETFSELRQIGLKKGFFEVASGPLVRSSYRADRVFKRDNLGLDV

Gene
lipA
Protein
Lipoyl synthase
Organism
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.742 kDa
Sequence
MGKLIDIPIVVESGQKYKTSQGVTAIKDGIKSSGQDHERLPKPKWLRIVNHTTPAYSQVKEQVQKHRLATVCEEAKCPNISECWSHGTATIMLMGAVCTRACRFCSVDTGNPHGWLDAEEPENTAETVALMNLDYVVLTSVNRDDLPDGGANHYAKTIRAIKKRSPRTKVEALTPDFQGSERDVAVLLDSGVDVFAQNVETVERLTHPVRDNRAGYQQTLNVLAFAKKYRPDVLTKTSLMLGLGETDEEIIQTMDDLRTHHVDILTLGQYLQPTKNHLPIARYVTPETFSELRQIGLKKGFFEVASGPLVRSSYRADRVFKRDNLGLDV

Gene
lipA
Protein
Lipoyl synthase
Organism
Legionella pneumophila (strain Lens)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.754 kDa
Sequence
MGKLIDIPIVVESGQKYKTSQGVTAIKDGIKSSGQDHERLPKPKWLRIVNHTTPAYSQVKEQVQKHRLATVCEEAKCPNISECWSHGTATIMLMGAVCTRACRFCSVDTGNPHGWLDAEEPENTAETVALMNLDYVVLTSVNRDDLPDGGANHYAKTIRAIKKRSPRTKVEALTPDFQGSERDVAVLLDSGLDVFAQNVETVERLTHPVRDNRAGYQQTLNVLAFAKKYRPDVLTKTSLMLGLGETDEEIIRTMDDLRAHHVDILTLGQYLQPTKNHLPIARYVTPETFSELRQIGLKKGFFEVASGPLVRSSYRADRVFKRDNLGLDV

Gene
lipA
Protein
Lipoyl synthase
Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.039 kDa
Sequence
MSAEPEGRRMLRLEVRNAQTPIERKPEWIKTRATMGPEYRQLHSLVKSEGLHTVCQEAGCPNIYECWEDREATFLIGGSQCTRRCDFCQIDTGKPAEFDRDEPRRVAESVARMGLRYSTVTGVARDDLEDEGAWLYAETIREIHRQSPGTGVEILVPDFSGDPELLGEVFGARPEVFAHNVETVPRIFKRIRPAFRYERSLDVIAQGRAAGLITKSNLILGMGEERQEISQALQDLHDAGTDIITITQYLRPSPRHLPVARWVRPDEFVELRDEAEAIGFLGVLAGPLVRSSYRAGRLWAQSMRAKGRTVPEELRHLADASLGFAQAVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.039 kDa
Sequence
MSAEPEGRRMLRLEVRNAQTPIERKPEWIKTRATMGPEYRQLHSLVKSEGLHTVCQEAGCPNIYECWEDREATFLIGGSQCTRRCDFCQIDTGKPAEFDRDEPRRVAESVARMGLRYSTVTGVARDDLEDEGAWLYAETIREIHRQSPGTGVEILVPDFSGDPELLGEVFGARPEVFAHNVETVPRIFKRIRPAFRYERSLDVIAQGRAAGLITKSNLILGMGEERQEISQALQDLHDAGTDIITITQYLRPSPRHLPVARWVRPDEFVELRDEAEAIGFLGVLAGPLVRSSYRAGRLWAQSMRAKGRTVPEELRHLADASLGFAQAVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.659 kDa
Sequence
MSAAPEGRRMLRLEVRNAETPIERKPEWIKTKARMGPEYQALQQLVKTEDLHTVCQEAACPNIYECWEDREATFLIGGSQCTRRCDFCQIDTGKPADYDTDEPRRVADSVRRMGLRYATVTGVARDDLPDEGAWLHAETVRRIHADNPGTGVEILATDFSGNPDLLAEVFSSRPEVFAHNVETVPRIFKRIRPAFRYERSLDVITQGRDADLITKSNLILGMGETREEVSEALADLHDAGCDIITVTQYLRPSPRHLPVARWVRPEEFVEIKAEAEAIGFLGVLAGPLVRSSYRAGRLYAQSMSAKGRELPASLAHLADPANGFAQAVG

Gene
lipA
Protein
Lipoyl synthase
Organism
Burkholderia mallei (strain NCTC 10247)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.459 kDa
Sequence
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATSSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALAILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Burkholderia mallei (strain NCTC 10229)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.459 kDa
Sequence
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATSSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALAILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Burkholderia mallei (strain ATCC 23344)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.459 kDa
Sequence
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATSSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALAILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Burkholderia mallei (strain SAVP1)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.459 kDa
Sequence
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATSSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALAILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Burkholderia pseudomallei (strain 1106a)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.429 kDa
Sequence
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATGSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALAILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Burkholderia pseudomallei (strain 1710b)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.429 kDa
Sequence
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATGSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALAILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Burkholderia pseudomallei (strain 668)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.429 kDa
Sequence
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATGSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALAILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Burkholderia pseudomallei (strain K96243)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.429 kDa
Sequence
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATGSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALAILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Length
329 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.487 kDa
Sequence
MTDLTATPAPAEPAASAYDPTAKQKAQAKTARIPIKIVPIEKLKKPEWIRVKAATGSSRFNEIKTILREHNLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDADEPKNLARTIAALKLKYVVITSVDRDDLRDGGAGHFVECIREVREQSPATRIEILTPDFRGRLDRALEILNAAPPDVMNHNLETVPRLYKEARPGSDYAHSLKLLKDFKALHPDVATKSGLMVGLGETTDEILQVMRDLRAHDVDMLTIGQYLQPSEHHLPVREYVHPDTFKMYEEEAYKMGFTHAAVGAMVRSSYHADLQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Length
328 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.964 kDa
Sequence
MSAVAPDGRKMLRLEVRNAQTPIERKPEWIKTRAKMGPEYTKMQNLVKSEGLHTVCQEAGCPNIYECWEDREATFLIGGDQCTRRCDFCQIDTGKPEALDRDEPRRVGESVVTMDLNYATITGVARDDLEDGGAWLYAETVRQIHAQTAGREAGRTKVELLAPDFNAEPDQLAEVFSARPEVFAHNVETVPRIFKRIRPGFRYERSLKVITEARDYGLVTKSNLILGMGETREEVSEALRQLHDAGCELITITQYLRPSVRHHPVERWVKPHEFVELKEEAEEIGFSGVMSGPLVRSSYRAGRLYQMAMELRQSAAPQGGAQVASQAV

Gene
lipA
Protein
Lipoyl synthase
Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Length
328 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.964 kDa
Sequence
MSAVAPDGRKMLRLEVRNAQTPIERKPEWIKTRAKMGPEYTKMQNLVKSEGLHTVCQEAGCPNIYECWEDREATFLIGGDQCTRRCDFCQIDTGKPEALDRDEPRRVGESVVTMDLNYATITGVARDDLEDGGAWLYAETVRQIHAQTAGREAGRTKVELLAPDFNAEPDQLAEVFSARPEVFAHNVETVPRIFKRIRPGFRYERSLKVITEARDYGLVTKSNLILGMGETREEVSEALRQLHDAGCELITITQYLRPSVRHHPVERWVKPHEFVELKEEAEEIGFSGVMSGPLVRSSYRAGRLYQMAMELRQSAAPQGGAQVASQAV

Gene
lipA
Protein
Lipoyl synthase
Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Length
328 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.707 kDa
Sequence
MSNDLTSESKTANRAAGEKFRDADKLAHIPIKVVSSTKATMLRKPSWLRIKLPKSSERIDNIKANLRKNDLHSVCEEASCPNLSECFNHGTATFMILGDICTRRCPFCDVGHGRPLAPKSDEPKKLANSLKDMGLKYVVITSVDRDDLRDGGAQQFADCVKEIGEQAPNTKVEILVPDFRGRMDRALEILNQNPPHVFNHNMETAPRLYTKVRPGANYQWSLDLLKRFGEANPDVTTKSGLMVGLGETNEEILEVMQDLRDHGVTMLTVGQYLQPSKDHLAVERYVHPDDFAMFEREAKKMGYEHAACGPLVRSSYHADKQAAGEEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Frankia alni (strain ACN14a)
Length
328 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.363 kDa
Sequence
MSAVAPEGRPLLRLEARNAQTPIERKPPWIRTRMRTGPEYSDVKGLVRAAGLHTVCEEAGCPNIYECWEDREATFLIGGDVCTRRCDFCQIDSGRPTPLDRDEPRRVAESVRTMGLRYATVTGVARDDLADGGSWLYGETVRQIHALSAGTGVEVLIPDFGGRADQLDEVFGAAPEVLAHNLETVPRIFKRIRPAFRYERSLDVLRQARAAGLVTKSNLILGLGETAEEIHAAMRDLHAAGCELLTVTQYLRPTPRHHPVERWVRPEEFLDWERVGAELGFSGVMSGPLVRSSYRAGRLYQQAITARGEGHTAASDLPKSVLETSHTQ

Gene
lipA
Protein
Lipoyl synthase
Organism
Deinococcus geothermalis (strain DSM 11300)
Length
328 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.762 kDa
Sequence
MTQQAKEPKFIKNGIYRKDAVPVRDKKPEWLKVTIPTGQVYGEVRKIVKEHRLHTVCEEAMCPNIGECWSRGTATFMLMGHICTRACRFCAVDTGNPMGKLDLEEPAHVAESVRLMGLKYVVLTSVDRDDLPDGGAYHFAKTVTAIKRENPGTRVEALTPDFGGNPHCVDLVLESGVDVYAQNLETVRRLTHPVRDIRASYERTLGVLKHAKQSRPDVITKTSIMLGLGETREELREAMLDCRAHGVDVITFGQYLRPTMHHLPVERYVSPAEFDEIREEGLSLGFLEVVAGPLVRSSYKAEQIVMDKPGNLPEHLAHLEGKEQLSLI

Gene
lipA
Protein
Lipoyl synthase
Organism
Variovorax paradoxus (strain S110)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.638 kDa
Sequence
MSTTEVVRDAQSAENYNPLAKQKAAAKLSRIPVKVVQQGEVLKKPEWIRVKAGSPTTRFYEIKQILRESNLHTVCEEASCPNIGECFGNGTATFMIMGDKCTRRCPFCDVGHGRPDPLDKDEPLNLAKTIAKLRLKYVVITSVDRDDLRDGGSQHFVDCITNIRELSPMTQIEILVPDFRGRDDRALEILKAAPPDVMNHNLETAPRLYKEARPGSDYQFSLNLLKKFKALHPQVPTKSGIMVGLGETDEEILQVMRDMRAHDIDMLTIGQYLSPSGSHLPVRRYVHPDTFKMFEEEAYKMGFSHAAVGAMVRSSYHADQQAHAAGV

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.245 kDa
Sequence
MAVVLDTLKNDPRPVRLRHPEKAHRPDQPVQAKKPDWIRVKAPGSRAWSETQKIVREHGLVTVCEEAGCPNIGECWEKRHATFMIMGDTCTRACAFCNVRTGLPDALDLGEPDKIADSVAKLGLHHVVITSVDRDDLRDGGAEHFARTIAAIRRASPGTTVEILTPDFLRKDGALEVVVAAKPDVFNHNLETVPAKYLTVRPGARYFHSVRLLQRVKELDPAIFTKSGIMVGLGEERNEVLQLMDDLRSADVDFLTIGQYLQPSKKHHEVVRFVPPDEFKAYETTAYAKGFLLVSATPLTRSSHHAGEDFARLQAARLAKLSPALSA

Gene
lipA
Protein
Lipoyl synthase
Organism
Francisella philomiragia subsp. philomiragia (strain ATCC 25017)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.092 kDa
Sequence
MKEISNIKVKIESGTKYTTDHGFHAVKDGIRNKKENSVHIRKPEWLKVKKQDSKEYLKVKSITKKHRLSTVCEEAKCPNINECWSHGTATIMLMGAVCTRACKFCSVDTGNPKGWLDKEEPQNTAESVKLMNLEYVVLTSVDRDDLVDGGAGHYAATITAIKNLDENIKVEALTPDFAGVKENVDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLEFLRYVKQKSPNILTKTSIMVGLGETDEEIYKTMDDARSVGVDIITLGQYMQPTKHHLSVERFVTPQQFEEYRRVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL

Gene
lipA
Protein
Lipoyl synthase
Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.84 kDa
Sequence
MKEISGIKVKVESGSKYTTDHGFHAVKDGIRNKKENAVHVRKPDWLKVQKQDSKEYLKVKSITKKHKLSTVCEEARCPNINECWSHGTATIMLMGSVCTRACKFCSVDTGNPKGWLDKDEPMNAAESVKLMGLEYVVLTSVDRDDLEDGGAGHYAATITAIKNLDENIKVEALTPDFAGINENIDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLNFLKYVKQKSPNVLTKTSIMVGLGETDEEIYKTMDDARSVGVDIITLGQYMQPTKHHLSVERFVTPQQFEEYRKVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL

Gene
lipA
Protein
Lipoyl synthase
Organism
Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.866 kDa
Sequence
MKEISGIKVKVESGSKYTTDHGFYAVKDGIRNKKENAVHVRKPDWLKVQKQDSKEYLKVKSITKKHKLSTVCEEARCPNINECWSHGTATIMLMGSVCTRACKFCSVDTGNPKGWLDKDEPMNAAESVKLMGLEYVVLTSVDRDDLEDGGAGHYAATITAIKNLDENIKVEALTPDFAGINENIDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLNFLKYVKQKSPNVLTKTSIMVGLGETDEEIYKTMDDARSVGVDIITLGQYMQPTKHHLSVERFVTPQQFEEYRKVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL

Gene
lipA
Protein
Lipoyl synthase
Organism
Francisella tularensis subsp. holarctica (strain LVS)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.866 kDa
Sequence
MKEISGIKVKVESGSKYTTDHGFYAVKDGIRNKKENAVHVRKPDWLKVQKQDSKEYLKVKSITKKHKLSTVCEEARCPNINECWSHGTATIMLMGSVCTRACKFCSVDTGNPKGWLDKDEPMNAAESVKLMGLEYVVLTSVDRDDLEDGGAGHYAATITAIKNLDENIKVEALTPDFAGINENIDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLNFLKYVKQKSPNVLTKTSIMVGLGETDEEIYKTMDDARSVGVDIITLGQYMQPTKHHLSVERFVTPQQFEEYRKVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL

Gene
lipA
Protein
Lipoyl synthase
Organism
Francisella tularensis subsp. mediasiatica (strain FSC147)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.854 kDa
Sequence
MKEISGIKVKVESGSKYTTDHGFHAVKDGIRNKKENAVHVRKPDWLKVQKQDSKEYLKVKSITKKHKLSTVCEEARCPNINECWSHGTATIMLMGSVCTRACKFCSVDTGNPKGWLDKDEPMNAAESVKLMGLEYVVLTSVDRDDLEDGGAGHYAATITAIKNLDENIKVEALTPDFAGINENIDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLNFLKYVKQKSPNVLTKTSIMVGLGETDEEIYKTMDDARSVGIDIITLGQYMQPTKHHLSVERFVTPQQFEEYRKVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL

Gene
lipA
Protein
Lipoyl synthase
Organism
Francisella tularensis subsp. novicida (strain U112)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.84 kDa
Sequence
MKEISGIKVKVESGSKYTTDHGFHAVKDGIRNKKENAVHVRKPDWLKVQKQDSKEYLKVKSITKKHKLSTVCEEARCPNINECWSHGTATIMLMGSVCTRACKFCSVDTGNPKGWLDKDEPMNAAESVKLMGLEYVVLTSVDRDDLEDGGAGHYAATITAIKNLDENIKVEALTPDFAGINENIDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLNFLKYVKQKSPNVLTKTSIMVGLGETDEEIYKTMDDARSVGVDIITLGQYMQPTKHHLSVERFVTPQQFEEYRKVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL

Gene
lipA
Protein
Lipoyl synthase
Organism
Francisella tularensis subsp. holarctica (strain OSU18)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.866 kDa
Sequence
MKEISGIKVKVESGSKYTTDHGFYAVKDGIRNKKENAVHVRKPDWLKVQKQDSKEYLKVKSITKKHKLSTVCEEARCPNINECWSHGTATIMLMGSVCTRACKFCSVDTGNPKGWLDKDEPMNAAESVKLMGLEYVVLTSVDRDDLEDGGAGHYAATITAIKNLDENIKVEALTPDFAGINENIDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLNFLKYVKQKSPNVLTKTSIMVGLGETDEEIYKTMDDARSVGVDIITLGQYMQPTKHHLSVERFVTPQQFEEYRKVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL

Gene
lipA
Protein
Lipoyl synthase
Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.84 kDa
Sequence
MKEISGIKVKVESGSKYTTDHGFHAVKDGIRNKKENAVHVRKPDWLKVQKQDSKEYLKVKSITKKHKLSTVCEEARCPNINECWSHGTATIMLMGSVCTRACKFCSVDTGNPKGWLDKDEPMNAAESVKLMGLEYVVLTSVDRDDLEDGGAGHYAATITAIKNLDENIKVEALTPDFAGINENIDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLNFLKYVKQKSPNVLTKTSIMVGLGETDEEIYKTMDDARSVGVDIITLGQYMQPTKHHLSVERFVTPQQFEEYRKVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL

Gene
lipA
Protein
Lipoyl synthase
Organism
Francisella tularensis subsp. tularensis (strain WY96-3418)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.84 kDa
Sequence
MKEISGIKVKVESGSKYTTDHGFHAVKDGIRNKKENAVHVRKPDWLKVQKQDSKEYLKVKSITKKHKLSTVCEEARCPNINECWSHGTATIMLMGSVCTRACKFCSVDTGNPKGWLDKDEPMNAAESVKLMGLEYVVLTSVDRDDLEDGGAGHYAATITAIKNLDENIKVEALTPDFAGINENIDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLNFLKYVKQKSPNVLTKTSIMVGLGETDEEIYKTMDDARSVGVDIITLGQYMQPTKHHLSVERFVTPQQFEEYRKVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas aeruginosa (strain PA7)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.775 kDa
Sequence
MSTVVEKSGEAKPGKVEVGVKLRGAEKVARIPVKIIPTEELPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDVDEPTNLAIAIADLRLKYVVITSVDRDDLRDGGAQHFADCLREIRKLSPGIQLETLVPDYRGRMDIALEITANEPPDVFNHNLETVPRLYRSSRPGSDFEWSLDLLQKFKQMVPHVPTKSGLMLGLGETDEEVIEVMQRMREHDIDMLTLGQYLQPSRNHLPVQRFVHPDTFAWFAEEGERMGFKNVASGPLVRSSYHADQQAHGNKIG

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas aeruginosa (strain LESB58)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.733 kDa
Sequence
MSTVVEKSGEAKPGKVEVGVKLRGAEKVARIPVKIIPTEELPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDVDEPTNLAIAIADLRLKYVVITSVDRDDLRDGGAQHFADCLREIRKLSPGIQLETLVPDYRGRMDIALEITANEPPDVFNHNLETVPRLYRSSRPGSDFEWSLDLLQKFKQMVPHVPTKSGLMLGLGETDDEVIEVMQRMREHDIDMLTLGQYLQPSRNHLPVQRFVHPDTFAWFAEEGEKMGFKNVASGPLVRSSYHADQQAHGNKIG

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.733 kDa
Sequence
MSTVVEKSGEAKPGKVEVGVKLRGAEKVARIPVKIIPTEELPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDVDEPTNLAIAIADLRLKYVVITSVDRDDLRDGGAQHFADCLREIRKLSPGIQLETLVPDYRGRMDIALEITANEPPDVFNHNLETVPRLYRSSRPGSDFEWSLDLLQKFKQMVPHVPTKSGLMLGLGETDDEVIEVMQRMREHDIDMLTLGQYLQPSRNHLPVQRFVHPDTFAWFAEEGEKMGFKNVASGPLVRSSYHADQQAHGNKIG

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.733 kDa
Sequence
MSTVVEKSGEAKPGKVEVGVKLRGAEKVARIPVKIIPTEELPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKPLDVDEPTNLAIAIADLRLKYVVITSVDRDDLRDGGAQHFADCLREIRKLSPGIQLETLVPDYRGRMDIALEITANEPPDVFNHNLETVPRLYRSSRPGSDFEWSLDLLQKFKQMVPHVPTKSGLMLGLGETDDEVIEVMQRMREHDIDMLTLGQYLQPSRNHLPVQRFVHPDTFAWFAEEGEKMGFKNVASGPLVRSSYHADQQAHGNKIG

Gene
lipA
Protein
Lipoyl synthase
Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.047 kDa
Sequence
MSEIKTDDPKRGIKLRGADKTARIPIKVVPLQEKLKKPEWIRAKLPSRKFFEIKDILREQKMHTVCEEASCPNIGECFSKGTATFMIMGDICTRRCPFCDVGHGRPNMLDPDEPKNLAESVKAMNLRYVVITSVDRDDLRDGGAQHFADCIKAIRETSPNTKIEILVPDFRGRLDIALKILAETPPDVMNHNLETHPSLYRKARPGANYQHSLDLLKRYKEMMPHIPTKSGIMVGLGETDEDVREIMRDMRAHNIEMITIGQYLQPSDGHLPVLRYVTPEQFKIFEKEAYELGFTNAAIGAMVRSSYHADEQAAEALRESHGGCGHH

Gene
lipA
Protein
Lipoyl synthase
Organism
Neisseria gonorrhoeae (strain NCCP11945)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.047 kDa
Sequence
MSEIKTDDPKRGIKLRGADKTARIPIKVVPLQEKLKKPEWIRAKLPSRKFFEIKDILREQKMHTVCEEASCPNIGECFSKGTATFMIMGDICTRRCPFCDVGHGRPNMLDPDEPKNLAESVKAMNLRYVVITSVDRDDLRDGGAQHFADCIKAIRETSPNTKIEILVPDFRGRLDIALKILAETPPDVMNHNLETHPSLYRKARPGANYQHSLDLLKRYKEMMPHIPTKSGIMVGLGETDEDVREIMRDMRAHNIEMITIGQYLQPSDGHLPVLRYVTPEQFKIFEKEAYELGFTNAAIGAMVRSSYHADEQAAEALRESHGGCGHH

Gene
lipA
Protein
Lipoyl synthase
Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.033 kDa
Sequence
MSEIKTDDPKRGIKLRGADKTARIPIKVVPLQEKLKKPEWIRAKLPSRKFFEIKDILREQKMHTVCEEASCPNIGECFSKGTATFMIMGDICTRRCPFCDVGHGRPNMLDPDEPKNLAESVKAMNLRYVVITSVDRDDLRDGGAQHFADCIKAIRETSPNTKIEILVPDFRGRLDIALKILAETPPDVMNHNLETHPSLYRKARPGANYQHSLDLLKRYKEMMPHIPTKSGIMVGLGETDEDVREIMRDMRAHNIEMITIGQYLQPSDGHLPVLRYVTPEQFKIFEKEAYELGFSNAAIGAMVRSSYHADEQAAEALRESHGGCGHH

Gene
lipA
Protein
Lipoyl synthase
Organism
Neisseria meningitidis serogroup B (strain MC58)
Length
327 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.061 kDa
Sequence
MSEIKTDDPKRGIKLRGADKTARIPIKVVPLQEKLKKPEWIRAKLPSRKFFEIKDILREQKMHTVCEEASCPNIGECFSKGTATFMIMGDICTRRCPFCDVGHGRPNMLDPDEPRNLAESVKAMNLRYVVITSVDRDDLRDGGAQHFADCIKAIRETSPNTKIEILVPDFRGRLDIALKILAETPPDVMNHNLETHPSLYRKARPGANYQHSLDLLKRYKEMMPHIPTKSGIMVGLGETDEDVREIMRDMRAHNIEMITIGQYLQPSDGHLPVLRYVTPEQFKIFEKEAYELGFSNAAIGAMVRSSYHADEQAAEALRESHGGCGHH

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidovorax ebreus (strain TPSY)
Length
326 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.542 kDa
Sequence
MSTPDVVREAQSTEAYNPLAKQKAAAKLSRIPIKVEQGEVLKKPEWIRVKAGSPTTRFYEIKNILREHKLHTVCEEASCPNIGECFGRGTATFMIMGDKCTRRCPFCDVGHGRPDPLDKDEPLNLAKTIAALRLKYVVITSVDRDDLRDGGSGHFVECIQRTRELSPSTQIEILTPDFRGRDDRALEILKAAPPDVMNHNLETVPRLYKEARPGSDYQFSLNLLKKFKQLHPGVPTKSGLMVGLGETDEEILEVMRDMRAHGIEMLTIGQYLAPSNSHLPVRRYVHPDTFKMFEEEAYKMGFSHAAVGAMVRSSYHADQQAHAAGV

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidovorax sp. (strain JS42)
Length
326 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.542 kDa
Sequence
MSTPDVVREAQSTEAYNPLAKQKAAAKLSRIPIKVEQGEVLKKPEWIRVKAGSPTTRFYEIKNILREHKLHTVCEEASCPNIGECFGRGTATFMIMGDKCTRRCPFCDVGHGRPDPLDKDEPLNLAKTIAALRLKYVVITSVDRDDLRDGGSGHFVECIQRTRELSPSTQIEILTPDFRGRDDRALEILKAAPPDVMNHNLETVPRLYKEARPGSDYQFSLNLLKKFKQLHPGVPTKSGLMVGLGETDEEILEVMRDMRAHGIEMLTIGQYLAPSNSHLPVRRYVHPDTFKMFEEEAYKMGFSHAAVGAMVRSSYHADQQAHAAGV

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidovorax ebreus (strain TPSY)
Length
326 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.542 kDa
Sequence
MSTPDVVREAQSTEAYNPLAKQKAAAKLSRIPIKVEQGEVLKKPEWIRVKAGSPTTRFYEIKNILREHKLHTVCEEASCPNIGECFGRGTATFMIMGDKCTRRCPFCDVGHGRPDPLDKDEPLNLAKTIAALRLKYVVITSVDRDDLRDGGSGHFVECIQRTRELSPSTQIEILTPDFRGRDDRALEILKAAPPDVMNHNLETVPRLYKEARPGSDYQFSLNLLKKFKQLHPGVPTKSGLMVGLGETDEEILEVMRDMRAHGIEMLTIGQYLAPSNSHLPVRRYVHPDTFKMFEEEAYKMGFSHAAVGAMVRSSYHADQQAHAAGV

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidovorax sp. (strain JS42)
Length
326 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.542 kDa
Sequence
MSTPDVVREAQSTEAYNPLAKQKAAAKLSRIPIKVEQGEVLKKPEWIRVKAGSPTTRFYEIKNILREHKLHTVCEEASCPNIGECFGRGTATFMIMGDKCTRRCPFCDVGHGRPDPLDKDEPLNLAKTIAALRLKYVVITSVDRDDLRDGGSGHFVECIQRTRELSPSTQIEILTPDFRGRDDRALEILKAAPPDVMNHNLETVPRLYKEARPGSDYQFSLNLLKKFKQLHPGVPTKSGLMVGLGETDEEILEVMRDMRAHGIEMLTIGQYLAPSNSHLPVRRYVHPDTFKMFEEEAYKMGFSHAAVGAMVRSSYHADQQAHAAGV

Gene
lipA
Protein
Lipoyl synthase
Organism
Aeromonas salmonicida (strain A449)
Length
326 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
37.008 kDa
Sequence
MSKPVRMEPGVKLRDGDKMALIPVKFMPDPNEEVLRKPDWMRIKLPPSSQKIEHIKSTLRKNKLHSVCEEASCPNLAECFNHGTATFMIMGAICTRRCPFCDVAHGRPLALDPDEPQKLALTIKEMGLKYVVITSVDRDDLRDGGAQHFADCIKQIREHSPQTRIEILTPDFRGRMEQALEVFRETPPDVFNHNLETAPRMYRVARPGADYKWSLELLRRIKEMHPHVPTKSGVMMGLGETNEEIVQVLKDLREHGVNMLTLGQYLQPSRHHLPVKRYVPPAEFDELKDVAMGLGFSHAACGPFVRSSYHADLQAKGEEVVGYKAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Delftia acidovorans (strain DSM 14801 / SPH-1)
Length
326 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.512 kDa
Sequence
MTTNTVVREAQSQAEYNPLAKQKAAAKLSRIPIKVEHGEALKKPDWIRVKAGSPTTRFYEIKDILRANKLHTVCEEASCPNIGECFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDTNEPLNLAKTIAELRLKYVVITSVDRDDLRDGGSGHFVECIKNIRELSPLTQIEILVPDFRGRDDRALEILKAAPPDVMNHNLETAPRLYKEARPGSDYQFSLNLLKKFKALHPKVPTKSGIMVGLGETDEEILQVMRDMRAHDIDMLTIGQYLAPSNSHLPVRRYVHPDTFKMFEEEAYKMGFTHAAVGAMVRSSYHADQQAHAAGV

Gene
lipA
Protein
Lipoyl synthase
Organism
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Length
326 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.515 kDa
Sequence
MSAVAPDGRKMLRLEVRNSQTPIERKPEWIKTRAKMGPEYKQLQQLVKGEGLHTVCQEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPQALDRDEPRRVGESVVTMDLNYATITGVARDDLEDGGAWLYAETVRQIHTLTAEREAGATKVELLIPDFNAEPEQLAEVFSSRPEVLAHNVETVPRIFKRIRPGFRYERSLEVITRAREAGLITKSNLILGMGETREEVSEALQDLYDAGCELITITQYLRPSVRHHPVERWVKPHEFVELKDEADAIGYSGVMSGPLVRSSYRAGRLFQQAMEARGVAAAGSAQAAQAV

Gene
lipA
Protein
Lipoyl synthase
Organism
Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1)
Length
326 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.155 kDa
Sequence
MVTRVLIDHRQGGRHEAGVRHPEKQHRPDNPSQPKPSWIRVKAPNHPVYHQTQALMRENRLTTVCEEAACPNIGECWSQRHATMMIMGDTCTRACSFCNVKTGLPHALDGDEPARVADAVARLGLRHVVITSVDRDDLNDGGAAHIAAVIKAVRLAAPETTIEVLTPDFLRKPGAAETVAEARPDVFNHNLETVPRLYPAIRPGARYFQSLRLLDQVKRLDPSIFTKSGLMVGLGEDRAEIAQVMDDLRIAEVDFITLGQYLQPTPKHAAVDRFVTPDEFSDYASMARSKGFLMVSSSPLTRSSYHADADFAALRAARMEQQQRIA

Gene
lipA
Protein
Lipoyl synthase
Organism
Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.805 kDa
Sequence
MPPLADASTETLSPAEQAAVRHPEKAHRPDQPIARKPDWIRVKAPGSPEWVETQKIVKEHKLVTVCEEAGCPNIGECWAKKHATFMIMGDTCTRACAFCNVKTGLPNGLDPHEPAHIADAVQKLGLSHVVITSVDRDDLADGGAEHFAQVIRAIREASPKTTIEVLTPDFLRKDGALEIVVAARPDVFNHNLETVPAKYLSVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGETRNEVLQLMDDLRTADVDFLTIGQYLQPTRKHHAVEAFITPDEFAAYAEVANAKGFLLVSASPLTRSSHHAGEDFARLKAARLERLGR

Gene
lipA
Protein
Lipoyl synthase
Organism
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.161 kDa
Sequence
MATVIDTLKARGSEDRAARHPEKQNRPDTPVLRKPEWLRVRAPGSGQYNETKGIVREHKLHTVCEEAACPNIGECWSQKHATMMIMGEICTRACAFCNVTTGLPTQLDPDEPRRVAEAVAKMGLKHVVITSVDRDDLLDGGARHFAEVVTSIRAAAPGTTIEILTPDFLRKDGAENVVIDSKPDVFNHNLETVPRLYLKIRPGARYYNSLRLLDRVKQRDPSQFTKSGLMVGLGETKEEVMQVMDDMRSAGVDFITIGQYLQPTRKHAAIDRFVTPEEFKAYEAIARAKGFLMVSSSPLTRSSHHAGEDFAKLQAARRALDARTA

Gene
lipA
Protein
Lipoyl synthase
Organism
Caulobacter vibrioides (strain NA1000 / CB15N)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.161 kDa
Sequence
MATVIDTLKARGSEDRAARHPEKQNRPDTPVLRKPEWLRVRAPGSGQYNETKGIVREHKLHTVCEEAACPNIGECWSQKHATMMIMGEICTRACAFCNVTTGLPTQLDPDEPRRVAEAVAKMGLKHVVITSVDRDDLLDGGARHFAEVVTSIRAAAPGTTIEILTPDFLRKDGAENVVIDSKPDVFNHNLETVPRLYLKIRPGARYYNSLRLLDRVKQRDPSQFTKSGLMVGLGETKEEVMQVMDDMRSAGVDFITIGQYLQPTRKHAAIDRFVTPEEFKAYEAIARAKGFLMVSSSPLTRSSHHAGEDFAKLQAARRALDARTA

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.878 kDa
Sequence
MASDSDLLDTKPAETRHPEKAHRPDQPTLRKPDWIRVRAPGSPEWAATNKIVKEHKLVTVCEEAGCPNIGECWAKKHATFMIMGDTCTRACAFCNVKTGLPRALDRNEPQRVADAVAKLGLSHVVITSVDRDDLSDGGARHFAEVIAAIRSLSPKTTIEVLTPDFLRKPGALEIVVAAKPDVFNHNLETVAGKYLGVRPGARYFHSLRLLQRVKELDPTLFTKSGIMLGLGEERQEVLQLMDDLRSADVDFMTIGQYLQPTKKHHAVARFVTPEEFNSYAEIGRAKGFLLMSSSPLTRSSHHAGEDFARLKAKRQALAPCAEAGQ

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium sp. (strain JLS)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.147 kDa
Sequence
MTVTPSGSNGAGSAAPEGRKLLRLEVRNAQTPIERKPPWIKTRARMGPEYKELKSLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGEQCTRRCDFCQIDTGKPSELDRDEPRRVAESVQAMGLRYSTVTGVARDDLPDGGAWLYAETVREIKRLNPNTGVELLIPDFNGDPALLAQVFESRPEVLAHNVETVPRIFKRIRPAFRYERSLAVLTAARDDNLVTKSNLILGMGETPDEVRTALVDLHEAGCDIITITQYLRPSPRHHPVERWVKPEEFVEFAQFAEGLGFAGVLSGPLVRSSYRAGRLYAQAARLKPAATPPVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium sp. (strain KMS)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.147 kDa
Sequence
MTVTPSGSNGAGSAAPEGRKLLRLEVRNAQTPIERKPPWIKTRARMGPEYKELKSLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGEQCTRRCDFCQIDTGKPSELDRDEPRRVAESVQAMGLRYSTVTGVARDDLPDGGAWLYAETVREIKRLNPNTGVELLIPDFNGDPALLAQVFESRPEVLAHNVETVPRIFKRIRPAFRYERSLAVLTAARDDNLVTKSNLILGMGETPDEVRTALVDLHEAGCDIITITQYLRPSPRHHPVERWVKPEEFVEFAQFAEGLGFAGVLSGPLVRSSYRAGRLYAQAARLKPAATPPVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium sp. (strain MCS)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.147 kDa
Sequence
MTVTPSGSNGAGSAAPEGRKLLRLEVRNAQTPIERKPPWIKTRARMGPEYKELKSLVKREGLHTVCEEAGCPNIFECWEDREATFLIGGEQCTRRCDFCQIDTGKPSELDRDEPRRVAESVQAMGLRYSTVTGVARDDLPDGGAWLYAETVREIKRLNPNTGVELLIPDFNGDPALLAQVFESRPEVLAHNVETVPRIFKRIRPAFRYERSLAVLTAARDDNLVTKSNLILGMGETPDEVRTALVDLHEAGCDIITITQYLRPSPRHHPVERWVKPEEFVEFAQFAEGLGFAGVLSGPLVRSSYRAGRLYAQAARLKPAATPPVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Maricaulis maris (strain MCS10)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.867 kDa
Sequence
MANLIDNTARSAASDARAARHPEKQKRADTPVLRKPDWIRVKAPLGKTFSETQKIVKDGGLVTVCEEAGCPNIGECWEQKHATFMILGDTCTRACSFCNVKTGLPAAVDTDEPRRVAEAVAQMGLNHVVITSVDRDDLDDGGAQHFVDVIEAIRAATPSTTIEILTPDFLRKPGAAEAVIDARPDVFNHNLETVPRLYLSIRPGARYFHSLRLLERVKDRDPAQFTKSGIMVGLGESKEEVMQVMDDMRSAGIDFLTIGQYLQPTRKHAAVDRFVHPDEFKAYETIARAKGFLMVSATPLTRSSHHAGDDFAKLRAAREQMMARG

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.464 kDa
Sequence
MTEITERIVPPPRKVAGVKESSAEKMARIPIKIIPMPAMRKPEWIRMKVPDSARFREIKQVLRENNLHTVCEEASCPNIGECFSGGTATFMILGDICTRRCPFCDVSHGKPLPPDANEPENLGRTIAQMRLKYVVITSVDRDDLRDGGAQHFVDCIAAVRAHSPQIKVEILVPDFRGRLDRAIHILKAAPPDVMNHNLETVPRLYKEARPGSDYQNSLDLLKEFGKLHPEVPTKSGLMLGLGETDEEILDVMRDLRAHNVTMLTLGQYLQPSPHHLPVKRFVTPQRFAEFERQALAMGFTHAACGPMVRSSYHADHQAQQAGVNF

Gene
lipA
Protein
Lipoyl synthase
Organism
Maricaulis maris (strain MCS10)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.867 kDa
Sequence
MANLIDNTARSAASDARAARHPEKQKRADTPVLRKPDWIRVKAPLGKTFSETQKIVKDGGLVTVCEEAGCPNIGECWEQKHATFMILGDTCTRACSFCNVKTGLPAAVDTDEPRRVAEAVAQMGLNHVVITSVDRDDLDDGGAQHFVDVIEAIRAATPSTTIEILTPDFLRKPGAAEAVIDARPDVFNHNLETVPRLYLSIRPGARYFHSLRLLERVKDRDPAQFTKSGIMVGLGESKEEVMQVMDDMRSAGIDFLTIGQYLQPTRKHAAVDRFVHPDEFKAYETIARAKGFLMVSATPLTRSSHHAGDDFAKLRAAREQMMARG

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.464 kDa
Sequence
MTEITERIVPPPRKVAGVKESSAEKMARIPIKIIPMPAMRKPEWIRMKVPDSARFREIKQVLRENNLHTVCEEASCPNIGECFSGGTATFMILGDICTRRCPFCDVSHGKPLPPDANEPENLGRTIAQMRLKYVVITSVDRDDLRDGGAQHFVDCIAAVRAHSPQIKVEILVPDFRGRLDRAIHILKAAPPDVMNHNLETVPRLYKEARPGSDYQNSLDLLKEFGKLHPEVPTKSGLMLGLGETDEEILDVMRDLRAHNVTMLTLGQYLQPSPHHLPVKRFVTPQRFAEFERQALAMGFTHAACGPMVRSSYHADHQAQQAGVNF

Gene
lipA
Protein
Lipoyl synthase
Organism
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.346 kDa
Sequence
MSTTETTGKSPAKVETGVKLRGAEKVARIPVKVIPTEELPRKPDWIRVRMPASPEVERIKQLLRQHKLHSVCEEASCPNLGECFAGGTATFMIMGDICTRRCPFCDVGHGRPNPLDPDEPKNLAVAVADLRLKYVVITSVDRDDLRDGGAQHFADCLREIRRLSPGTQLETLVPDYRGRMEIALDITAAEPPDVFNHNLETVPRLYKASRPGADFEWSLDLLEAFKKRVPAVPTKSGLMLGLGETDEEVIEVMKRMREHEIDMLTLGQYLQPSRNHLAVQRFVHPDTFAWFAEEGERMGFKNVTSGPLVRSSYHADQQAHGAKGD

Gene
lipA
Protein
Lipoyl synthase
Organism
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.458 kDa
Sequence
MSEQAQAKRKVQIGDKLRGADKVRTIPMVNEETGYQRKPDWIRVRVPANGEIQRIKSLLRKQKLHTVCEEAACPNLPECFGGGTATFMIMGDICTRRCAFCDVGFGRPNALDAQEPLHLAESVENLGLNYVVITSVDRDDLADGGAEHFAECIRQVRALTPETRIEILTPDFRPCLDTAVEILAETAPDVFNHNIETVPELYKHIRPGARYQHSLDLLKRYKALRPDVSTKSGIMVGLGETFEQVINTIKDLRTHDVDMITIGQYLQPSKHHAPVDRFVHPDEFREYARVANELGFTSVASGPMVRSSYHADLQHKGVDVGLYKP

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas stutzeri (strain A1501)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.503 kDa
Sequence
MSSVETAGKRPAKVEAGVKLRGAEKVARIPVKIIPTDELPKKPDWIRVRIPVSPEVDQIKQTLRKHKLHSVCEEASCPNLGECFSSGTATFMIMGDICTRRCPFCDVGHGRPNALDPDEPKNLAQAIADMRLKYVVITSVDRDDLRDGGAQHFADCLREIRKLSPSIQLETLVPDYRGRMEIALDITATEPPDVFNHNLETVPRLYKSSRPGSDFEWSLDLLEKFKQRVPGVPTKSGLMLGLGETDEEVIEVMQRMREHDIDMLTLGQYLQPSRNHLPVQRFVHPDTFAWFAEEGMKMGFKNVASGPLVRSSYHADQQAHGAKHD

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodospirillum centenum (strain ATCC 51521 / SW)
Length
325 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.757 kDa
Sequence
MPIAPDRVRHPEKANRPDNPIQRKPEWLRVKAPTSPEYGETRSLMRGLRLNTVCEEAACPNIGECWKKKHATFMILGAVCTRACAFCNVATGRPDQLDPHEPEKVAEAVAHLKLEHIVVTSVDRDDLEDGGAGHFARTIRAIRAAAPGTTIEVLTPDFMKKKGAVETVVEARPDVFNHNLETAPRLYPTIRPGARYFTSLQLLARVKEIDPSMFTKSGIMVGLGETKEEVFQVMDDLRAADVDFMTIGQYLAPTPKHAKVDRFVTPDEFAGYVTVGRGKGFLMVASSPLTRSSYHAGADFERLRAAREAKLAGRPVAAPEATSAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Length
324 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.021 kDa
Sequence
MNVAPEPGAAGAAAPQGRKLLRLEVRNAQTPIERKPPWIRTRARMGPEYTELKNLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAPLDRDEPRRVAESVHTMGLRYATVTGVARDDLPDGGAWLYAETVRAIKELNPSTGVELLIPDFNGKADQLGEVFEARPEVLAHNVETVPRVFKRIRPAFTYQRSLDVLTAARQFGLVTKSNLILGMGETPEEVRTALVDLHDAGCDIITITQYLRPSPRHHPVERWVRPEEFVEFAQYAEGLGFAGVLAGPLVRSSYRAGRLYEQARSRNTSGASNSG

Gene
lipA
Protein
Lipoyl synthase
Organism
Dichelobacter nodosus (strain VCS1703A)
Length
324 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.653 kDa
Sequence
MAEPIIVKGQKQNAMGVKRKGAEKVRHVAADAEHFEQERLKKPSWIRAKMPTGPEVMRMKAMMREQKLHSVCEEASCPNLGECFRFGTASFMIMGDICTRRCPFCDVAHGRPRPLNPFEPRNLAQTVYNLGLAHVVITSVDRDDLRDGGAAHFAACIREIRRVSPKMTIEILTPDFRGRAELAVQILSATPPDVFNHNLETIPRFYDVVRPGANYERSLHLLRDYKKACPKKIITKSGLMVGLGEEIEEILQVMQDLRSHDVDMLTVGQYLQPSVHHLPVKRYYTPEEFDFLAQEGKKMGFLHVASGAMVRSSYHADRSAQTVL

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium ulcerans (strain Agy99)
Length
324 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.021 kDa
Sequence
MNVAPEPGAAGAAAPQGRKLLRLEVRNAQTPIERKPPWIRTRARMGPEYTELKNLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAPLDRDEPRRVAESVHTMGLRYATVTGVARDDLPDGGAWLYAETVRAIKELNPSTGVELLIPDFNGKADQLGEVFEARPEVLAHNVETVPRVFKRIRPAFTYQRSLDVLTAARQFGLVTKSNLILGMGETPEEVRTALVDLHDAGCDIITITQYLRPSPRHHPVERWVRPEEFVEFAQYAEGLGFAGVLAGPLVRSSYRAGRLYEQARSRNTSGASNSG

Gene
lipA
Protein
Lipoyl synthase
Organism
Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107)
Length
324 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.03 kDa
Sequence
MSQKTPSPPGELKRDIRALKGASKVARIPVKVEPTTERQRKPHWIRAKAPIGPEVLRLKGLLREHRLHTVCEEASCPNLGECFGHGTATFLIMGNICTRRCPFCDVAHGRPDPLDAEEPMHLAQAIGAMGLRHVVVTSVDRDDLRDGGAAHFTHCIQAIRTQSPQTRIEVLVPDFRGRMDRALEALTAGPPDIFNHNLETVPRLYKAVRPGADYLWSLRLLARFKEDHPTVPTKSGLMLGLGEELAEVEQVMKDLRDHGCDMLTLGQYLQPSLYHLPVRRFVTPEEFDGLGDKAREMGFTHVASGPMVRSSYHADRQAAGESVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Sinorhizobium medicae (strain WSM419)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.283 kDa
Sequence
MVTVFDAVADRAQRVRHPEKAHRPDTEVLRKPDWIRVKAPTSKGYQETRSIVKSHNLVTVCEEAGCPNIGECWDKKHATFMIMGEICTRACAFCNVATGRPNALDLDEPVNVAKAVKQMGLSHVVITSVDRDDLEDGGAEHFERVIFAIREASPQTTIEILTPDFLRKPGALERVVAAKPDVFNHNLETVPSNYLTVRPGARYFHSIRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRTADVDFLTIGQYLQPTRKHHKVEKFVTPDEFKSYETVAYTKGFLMVSSSPLTRSSHHAGDDFARLKAAREKKLLAAAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidothermus cellulolyticus (strain ATCC 43068 / 11B)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.163 kDa
Sequence
MTAVTPDGRKLLRIEARNAQVPIERKPAWIRTRARMGPQYHALKELVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDTCSRNCSFCQISSGRPQPLDRDEPRRVAESVARMGLRYATVTGVTRDDLDDEGAWLYAQTVREIHHAVPGCGVELLTPDFHGRPELLDEVFSARPEVFAHNIETVPRIFKSIRPGFRYERSLDVLRAAHDAGLVTKSNLILGLGETRQEIRAALADLRSAGCDLVTITQYLRPSIRHHPVVRWVEPAEFEELAAEARELGFAGVMSGPLVRSSYRAGRLYRAAIASRTDRRTDGATTQAPQTP

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidothermus cellulolyticus (strain ATCC 43068 / 11B)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.163 kDa
Sequence
MTAVTPDGRKLLRIEARNAQVPIERKPAWIRTRARMGPQYHALKELVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDTCSRNCSFCQISSGRPQPLDRDEPRRVAESVARMGLRYATVTGVTRDDLDDEGAWLYAQTVREIHHAVPGCGVELLTPDFHGRPELLDEVFSARPEVFAHNIETVPRIFKSIRPGFRYERSLDVLRAAHDAGLVTKSNLILGLGETRQEIRAALADLRSAGCDLVTITQYLRPSIRHHPVVRWVEPAEFEELAAEARELGFAGVMSGPLVRSSYRAGRLYRAAIASRTDRRTDGATTQAPQTP

Gene
lipA
Protein
Lipoyl synthase
Organism
Agrobacterium fabrum (strain C58 / ATCC 33970)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.341 kDa
Sequence
MVTILDRTSSDEKRIRHPEKAHRPDTEVMRKPEWIRVKAPTSKGYHETRELVRSHKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNVATGKPNALDMDEPENVAKAVKQMGLSHVVITSVDRDDLADGGAEHFEKVIWAIRAASPTTTIEILTPDFLKKPGALERVVAAKPDVFNHNMETVPGNYLTVRPGARYFHSVRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRSADVDFLTIGQYLQPTRKHHKVEAFVTPEEFKSYETVAYAKGFLMVSSSPLTRSSHHAGDDFERLRAAREKKLLAAAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Agrobacterium radiobacter (strain K84 / ATCC BAA-868)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.223 kDa
Sequence
MVTILDRINPDAKRVRHPEKAHRPDTEVLRKPDWIRVKAPTSKGYAETRSIVKEHKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNVATGKPNALDMAEPENIAKAVKEMGLSHVVITSVDRDDLADGGAEHFEKVIWAIRAASPMTTIEILTPDFLKKPGALERVVAAKPDVFNHNMETVPGNYLTVRPGARYFHSVRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRTADVDFLTIGQYLQPTRKHHQVMSFVTPEEFKSYETVAYTKGFLMVASSPLTRSSHHAGDDFARLRAAREKKILLAAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Agrobacterium vitis (strain S4 / ATCC BAA-846)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.458 kDa
Sequence
MVTILDRTKPDDKRIRHPEKAHKPDTEVLRKPEWIRVKAPTSKGYQETRELVRSHKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNVATGKPNALDREEPANVAKAVRQMGLSHVVITSVDRDDLADGGAEHFEQVIWAIREASPATTIEILTPDFLKKPGALERVVAAKPDVFNHNMETVPGNYLTVRPGARYFHSVRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRTADVDFLTIGQYLQPTRKHHKVERFVTPEEFKSYEDIAYTKGFLMVASSPLTRSSHHAGDDFARLKANREKKLLAAAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Protochlamydia amoebophila (strain UWE25)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.51 kDa
Sequence
MMENSPKTRRLNILPDNPENTGDGVVGLGRFPSWLHRPLPKGNQLQITGQVINQNRLHTVCEEAKCPNLLECWTKKTATFLVMGKECSRNCGFCDIDFSKNPKPLDRSEPSRVALSVQQLGLKHVVITMVARDDLSDGGSSHLVEVIEAIRQTNEDVTIEVLTSDFEGNRKALSFVLQAKPEIFNHNIETVRRLTPRVRHKATYERTLSVLEQAAQKKYHSQLKVKSGIMVGLGETEEEIFETLLDLKRVGCEIVTIGQYLQPNRQKLLVKSFVHPDIFKKYEQYGLSIGIPHLYCGPFVRSSYNANLVLMRANQKEAIVNSE

Gene
lipA
Protein
Lipoyl synthase
Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.909 kDa
Sequence
MKPKFETVELLSPTGEVVELKVVKRGLAQARPEPVDRNKPAWIKAPLPTGPRYQALKAMVRELRLHTVCQEALCPNIGECWTHGTLTVMILGDICTRACKFCAVHTGNPKGLVDPEEPRRVAEAIARMGVRYVVLTSVDRDDLPDGGASHFAATIRAIKERAPGVLVEALTPDFQGDLKAVETVLAANPEVYAQNLETVRRLTPKVRDPRAGYEQTLKVLAHAKKVRPDILTKSSLMLGLGETEEEILEAMRDLRAAGVDILTLGQYLRPTPAHLPVARYVPPEDFKRYEAWGYELGFREVFAGPLVRSSYRADRVFLEATQR

Gene
lipA
Protein
Lipoyl synthase
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.909 kDa
Sequence
MKPKFETVELLSPTGEVVELKVVKRGLAQARPEPVDRNKPAWIKAPLPTGPRYQALKAMVRELRLHTVCQEALCPNIGECWTHGTLTVMILGDICTRACKFCAVHTGNPKGLVDPEEPRRVAEAIARMGVRYVVLTSVDRDDLPDGGASHFAATIRAIKERAPGVLVEALTPDFQGDLKAVETVLAANPEVYAQNLETVRRLTPKVRDPRAGYEQTLKVLAHAKKVRPDILTKSSLMLGLGETEEEILEAMRDLRAAGVDILTLGQYLRPTPAHLPVARYVPPEDFKRYEAWGYELGFREVFAGPLVRSSYRADRVFLEATQR

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhizobium etli (strain CIAT 652)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.083 kDa
Sequence
MVTILDTINPDAKRVRHPEKAHRPDTEVMRKPDWIRVKAPTSKGYAETRAIVKEHKLVTVCEEAGCPNIGECWDKKHATFMIMGEICTRACAFCNVATGKPNALDMAEPENVAKAVKEMGLSHVVITSVDRDDLEDGGAEHFEKVIWAIRAASPATTIEILTPDFLKKPGALERVVAAKPDVFNHNMETVAGNYLTVRPGARYFHSIRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRTADVDFLTIGQYLQPTRKHHKVESFVTPDEFKSYETVAYSKGFLMVASSPLTRSSHHAGDDFARLRAAREKKLLVAAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhizobium etli (strain CFN 42 / ATCC 51251)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.218 kDa
Sequence
MVTILDTINPDAKRVRHPEKAHRPDTEVMRKPDWIRVKAPTSKGYAETRAIVKEHKLVTVCEEAGCPNIGECWDKKHATFMIMGEICTRACAFCNVATGKPNALDMDEPENVAKAVREMGLSHVVITSVDRDDLEDGGAEHFEKVIWAIRSASPATTIEILTPDFLKKPGALERVVAAKPDVFNHNMETVAGNYLTVRPGARYFHSIRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRTADVDFLTIGQYLQPTRKHHKVESFVTPEEFKSYETVAYSKGFLMVASSPLTRSSHHAGDDFARLRAAREKKLLMAAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhizobium leguminosarum bv. viciae (strain 3841)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.188 kDa
Sequence
MVTILDTINPDAKRVRHPEKAHRPDTEVMRKPDWIRVKAPTSKGYAETRAIVKEHKLVTVCEEAGCPNIGECWDKKHATFMIMGEICTRACAFCNVATGKPNALDMAEPENVAKAVKEMGLSHVVITSVDRDDLEDGGAEHFEKVIWAIRAASPMTTIEILTPDFLKKPGALERVVAAKPDVFNHNMETVPGNYLTVRPGARYFHSVRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRTADVDFLTIGQYLQPTRKHHKVESFVTPDEFKSYETVAYSKGFLMVASSPLTRSSHHAGDDFARLRAAREKKLLMAAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhizobium leguminosarum bv. trifolii (strain WSM2304)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.142 kDa
Sequence
MVTILDTINPDAKRVRHPEKAHRPDTEVMRKPDWIRVKAPTSKGYAETRAIVKEHKLVTVCEEAGCPNIGECWDKKHATFMIMGEICTRACAFCNVATGKPNALDMAEPENVAKAVKEMGLSHVVITSVDRDDLEDGGAEHFEKVIWAIRAASPATTIEILTPDFLKKPGALERVVAAKPDVFNHNMETVPGNYLTVRPGARYFHSIRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRTADVDFLTIGQYLQPTRKHHKVESFVTPDEFKSYETVAYSKGFLMVASSPLTRSSHHAGDDFARLRAAREKKLLMAAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.865 kDa
Sequence
MKKNKDVLLKNKILKKLNIINIKNLDNIKEKLKKPDWIKIKIPVNTSRIYQIKNALRKNNLYSVCEEAHCPNLSECFNNGTATFMILGSICTRNCPFCAVFHGRPNPVNVEEPQKLSDTIFDMGINYVVITSVVRDDLYDGGAEHFVNCIKAIKNKNQVKIEILVPDFRGRIELILNIFNNALPDIFNHNIENVPRLYKKIRPGANYQRSLLLLESFKKKYCSVLTKSGLMLGLGEKDVEIIQVMKDLYSSGVTLLTVGQYLQPSIHHLPVKRYIPLSEFENIKKEALSIGFTNAFCGPFVRSSYHASFQSHLPIKNNDINNI

Gene
lipA
Protein
Lipoyl synthase
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.877 kDa
Sequence
MKKNKDVLLKNKILKKLNIINIKNLDNIKEKLKKPDWIKIKIPVNTSRIYQIKNALRKNNLYSVCEEAHCPNLSECFNNGTATFMILGSICTRNCPFCAVFHGRPNPVNVEEPQKLSDTIFDMGINYVVITSVVRDDLYDGGAEHFVNCIKAIKNKNQVKIEILVPDFRGRIELILNIFNKALPDIFNHNIENVPRLFKKIRPGANYQRSLLLLESFKKKYCSVLTKSGLMLGLGEKDVEIIQVMKDLYSSGVTLLTVGQYLQPSIHHLPVKRYIPLSEFENIKKEALSIGFTNAFCGPFIRSSYHASFQSHLPIKNNDINNI

Gene
lipA
Protein
Lipoyl synthase
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.865 kDa
Sequence
MKKNKDVLLKNKILKKLNIINIKNLDNIKEKLKKPDWIKIKIPVNTSRIYQIKNALRKNNLYSVCEEAHCPNLSECFNNGTATFMILGSICTRNCPFCAVFHGRPNPVNVEEPQKLSDTIFDMGINYVVITSVVRDDLYDGGAEHFVNCIKAIKNKNQVKIEILVPDFRGRIELILNIFNNALPDIFNHNIENVPRLYKKIRPGANYQRSLLLLESFKKKYCSVLTKSGLMLGLGEKDVEIIQVMKDLYSSGVTLLTVGQYLQPSIHHLPVKRYIPLSEFENIKKEALSIGFTNAFCGPFVRSSYHASFQSHLPIKNNDINNI

Gene
lipA
Protein
Lipoyl synthase
Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Length
323 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.662 kDa
Sequence
MSKIPAPDEKTSRSDSGSSILRKPDWLRVRSPGGAAFNETHGLIRKLGLATVCEEAACPNIGECWTKKQATVMILGEVCTRACAFCNVKTGHPDKVNPLEPGHVADVAAEMNLEHIVITSVDRDDLEDGGASQFVKVIEAVRARTPKTTIEILTPDFRGKPDHALDMIVKARPDVFNHNLETVPRLYPTIRPGARYFTSLRLLEKVRERDPSIFTKSGLMLGLGEDRLEVHQVMDDMRQADVDFLTLGQYLQPTPRHVRVEEFVTPDSFKAYAATARAKGFSMVASSPLTRSSYYAGADFARLKEARQKKLEKIAAKNSGKGA

Gene
lipA
Protein
Lipoyl synthase
Organism
Brucella abortus (strain S19)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.957 kDa
Sequence
MVTVLNTVNQSGRLRHPEKAHRPDNEVLKKPDWIRVKAPVSRGYGETREIVRSNKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNISTGIPNALDPNEPENIAKAVKQMGLTHVVITSVDRDDLADGGAHHFAEVIKAVREAAPATTIEILTPDFLRKEGALEIVVKARPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVKPDEFKSFETIGKTKGFLLVASSPLTRSSHHAGEDFAKLKAAREALYASRAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Brucella abortus (strain 2308)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.957 kDa
Sequence
MVTVLNTVNQSGRLRHPEKAHRPDNEVLKKPDWIRVKAPVSRGYGETREIVRSNKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNISTGIPNALDPNEPENIAKAVKQMGLTHVVITSVDRDDLADGGAHHFAEVIKAVREAAPATTIEILTPDFLRKEGALEIVVKARPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVKPDEFKSFETIGKTKGFLLVASSPLTRSSHHAGEDFAKLKAAREALYASRAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Brucella abortus biovar 1 (strain 9-941)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.957 kDa
Sequence
MVTVLNTVNQSGRLRHPEKAHRPDNEVLKKPDWIRVKAPVSRGYGETREIVRSNKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNISTGIPNALDPNEPENIAKAVKQMGLTHVVITSVDRDDLADGGAHHFAEVIKAVREAAPATTIEILTPDFLRKEGALEIVVKARPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVKPDEFKSFETIGKTKGFLLVASSPLTRSSHHAGEDFAKLKAAREALYASRAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Brucella canis (strain ATCC 23365 / NCTC 10854)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.957 kDa
Sequence
MVTVLNTVNQSGRLRHPEKAHRPDNEVLKKPDWIRVKAPVSRGYGETREIVRSNKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNISTGIPNALDPNEPENIAKAVKQMGLTHVVITSVDRDDLADGGAHHFAEVIKAVREAAPATTIEILTPDFLRKEGALEIVVKARPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVKPDEFKSFETIGKTKGFLLVASSPLTRSSHHAGEDFAKLKAAREALYASRAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Brucella melitensis biotype 2 (strain ATCC 23457)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.957 kDa
Sequence
MVTVLNTVNQSGRLRHPEKAHRPDNEVLKKPDWIRVKAPVSRGYGETREIVRSNKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNISTGIPNALDPNEPENIAKAVKQMGLTHVVITSVDRDDLADGGAHHFAEVIKAVREAAPATTIEILTPDFLRKEGALEIVVKARPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVKPDEFKSFETIGKTKGFLLVASSPLTRSSHHAGEDFAKLKAAREALYASRAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.957 kDa
Sequence
MVTVLNTVNQSGRLRHPEKAHRPDNEVLKKPDWIRVKAPVSRGYGETREIVRSNKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNISTGIPNALDPNEPENIAKAVKQMGLTHVVITSVDRDDLADGGAHHFAEVIKAVREAAPATTIEILTPDFLRKEGALEIVVKARPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVKPDEFKSFETIGKTKGFLLVASSPLTRSSHHAGEDFAKLKAAREALYASRAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.444 kDa
Sequence
MSKPVRVEPGVKMRDADKMALIPVQIIPTERDQMLRKPSWLKVKLPSSTERIDEIKQAMRSHGLHSVCEEASCPNLPECFNHGTASFMILGDICTRRCPFCDVAHGRPLPPDPEEAEKLGKTIRDMKVKYVVITSVDRDDLRDGGAQHFADCIREIREHSENNIQVEVLVPDFRGRMQVAIDILKGEAPDVFNHNLETVPRLYKAARPGANYQWSLDLLQKYKEVRPDIRTKSGLMVGLGETKEEILEVMKDLRAHDVDMLTIGQYLQPSRHHIPVARYVHPDEFEELRVAGVEMGFSHIASGPLVRSSYHADLQAAGETVR

Gene
lipA
Protein
Lipoyl synthase
Organism
Chelativorans sp. (strain BNC1)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.963 kDa
Sequence
MVTVLDTVSKPRPRHPEKAHRPDQEVLRKPDWIRVKAPTSRGYLETREIVKTNKLVTVCEEAGCPNIGECWDKKHATFMIMGEICTRACAFCNVATGIPGPLDPNEPANVAKAVREMGLNHVVITSVDRDDLNDGGAQHFADVIQAIRAATPQTTIEILTPDFLRKDGALELVVAAKPDVFNHNLETVPSKYLTVRPGARYFHSIRLLQRVKEIDPSIFTKSGIMVGLGEERNEVLQLMDDLRSADVDFITIGQYLQPTKKHHPVKKFVTPEEFKSYETIAYTKGFLMASSSPLTRSSHHAGEDFERLRAAREARLSLAKTA

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.702 kDa
Sequence
MKTLDENQAPSRQTPESHRRGAEKLSRIPVKVEPGAPLRKPDWIRVRAGSGDEVRRVKRLLRERGLHSVCEEAACPNLAECFGHGTATFMILGDICTRRCPFCDVAHGRPAPPDPAEPERLAETIALLRLRYVVITSVDRDDLRDGGAAHFAACIRALRTRSPALSVEILTPDFRGRMEIALDLLAADPPDVFNHNIETVPRLYRQARPGADYRQSLELLARFRDKVPGVPTKSGLMLGLGETLDEVREALRDLRGHGCEMLTLGQYLQPSRDHLPVVRYVPPAEFDELAGYARELGFASVASAPLVRSSYHADQQAAIIGR

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.702 kDa
Sequence
MKTLDENQAPSRQTPESHRRGAEKLSRIPVKVEPGAPLRKPDWIRVRAGSGDEVRRVKRLLRERGLHSVCEEAACPNLAECFGHGTATFMILGDICTRRCPFCDVAHGRPAPPDPAEPERLAETIALLRLRYVVITSVDRDDLRDGGAAHFAACIRALRTRSPALSVEILTPDFRGRMEIALDLLAADPPDVFNHNIETVPRLYRQARPGADYRQSLELLARFRDKVPGVPTKSGLMLGLGETLDEVREALRDLRGHGCEMLTLGQYLQPSRDHLPVVRYVPPAEFDELAGYARELGFASVASAPLVRSSYHADQQAAIIGR

Gene
lipA
Protein
Lipoyl synthase
Organism
Photobacterium profundum (strain SS9)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.335 kDa
Sequence
MSKPIKIEQGIKYRDADKMALIPVRNVAEEAPKEVLRKPAWMKIKLPSDSKRIQEIKSALRKNKLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLPPNAEEPSHLAQTIADMKLKYVVITSVDRDDLRDGGAQHFVDCIREIREKSPEIHIETLVPDFRGRMDRALDILQGTPPNVFNHNLETAPRLYRKARPGANYQWSLDLLKNFKEIHPEVPTKSGVMMGLGETKEEIIQVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEIALELGFTHAACGPFVRSSYHADLQAQGLEIK

Gene
lipA
Protein
Lipoyl synthase
Organism
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.587 kDa
Sequence
MVTLIDTISERQVRPRHPEKAHRPDAISPPKPDWIRVRAPTSRGYANTRNIVKENGLVTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVRTGLPDGLDPDEPAHVALAVQKLGLAHVVITSVDRDDLADGGAAHFAATIAAIRESCPTTTIEILTPDFLRKEGALEVVVAAKPDVFNHNLETVPSRYQSVRPGARYFHSVRLLQRVKEIDPTIFTKSGIMVGLGEERHEVLQVMDDLRSADVDFLTIGQYLQPTLKHHAVMRYVTPEEFDGYERIAFTKGFLMVSASPLTRSSHHAGEDFARLKAAREAKLQSAG

Gene
lipA
Protein
Lipoyl synthase
Organism
Gluconobacter oxydans (strain 621H)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.93 kDa
Sequence
MSQRITIDHRSAPALRHPEKAHRPDNPIQRKPSWIRVKAPNHPVYHETRALMRDAGLVTVCEEAACPNIGECWSQRHATMMIMGEICTRACAFCNVTTGLPKHLDEDEPRRVGEAVAKLGLKHVVITSVDRDDLEDGGAMHFARVIHAIRETSPQTTIEILTPDFLRKDGALEVVVAARPDVFNHNIETIPRLYPTIRPGARYYQSVRLLDGVKKLDPSIFTKSGLMLGLGEERMEVAQVMDDFRIADVDFLTLGQYLQPSAKHAAVEKFVTPDEFDGYAAAARSKGFLQVSASPLTRSSYHADSDFAKLQAARNSRLKESL

Gene
lipA
Protein
Lipoyl synthase
Organism
Psychromonas ingrahamii (strain 37)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.03 kDa
Sequence
MSNKPSQLTAGKKLRDADKMSHIPIKVVPSNKSTLLKKPSWMKIKLSSDNTRVNEIKAALRKNNLHSVCEEASCPNLNECFNHGTATFMILGDICTRRCPFCDVGHGKPLAVDANEPKKLAETIKDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRLLNPEIKIEILVPDFKGRMDKALACFEQDLPDVFNHNLETAPHLYKQVRPGADYKWSLKLLQKFKEKHPHIPTKSGLMVGLGETNEDIEQVLTDLRAHDVNMLTLGQYLQPSLDHLAVQRFVPPSEFDELGVKAKALGFDQAACGPLVRSSYHADLQASGQEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhizobium meliloti (strain 1021)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.096 kDa
Sequence
MVTVFDAVSDRAQRVRHPEKAHRPDTEVLRKPDWIRVKAPTSKGYQETRSIVKSHKLVTVCEEAGCPNIGECWDKKHATFMIMGEICTRACAFCNVATGKPNALDLDEPANVAKAVKQMGLSHVVITSVDRDDLDDGGAEHFEKVIFAIREASPETTIEILTPDFLRKPGALERVVAAKPDVINHNLETVPSNYLTVRPGARYFHSIRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRTADVDFLTIGQYLQPSRKHHKVEKFVTPEEFKSYETVAYTKGFLMVSSSPLTRSSHHAGDDFARLKAARERKLAAAE

Gene
lipA
Protein
Lipoyl synthase
Organism
Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.057 kDa
Sequence
MVTVLNTVNQSGRLRHPEKAHRPDNEVLKKPDWIRVKAPVSRGYGETREIVRSNKLVTVCEEAGCPNIRECWEKKHATFMIMGEICTRACAFCNISTGIPNALDPNEPENIAKAVKQMGLTHVVITSVDRDDLADGGAHHFAEVIKAVREAAPATTIEILTPDFLRKEGALEIVVKARPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVKPDEFKSFETIGKTKGFLLVASSPLTRSSHHAGEDFAKLKAAREALYASRAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Brucella suis (strain ATCC 23445 / NCTC 10510)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.957 kDa
Sequence
MVTVLNTVNQSGRLRHPEKAHRPDNEVLKKPDWIRVKAPVSRGYGETREIVRSNKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNISTGIPNALDPNEPENIAKAVKQMGLTHVVITSVDRDDLADGGAHHFAEVIKAVREAAPATTIEILTPDFLRKEGALEIVVKARPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVKPDEFKSFETIGKTKGFLLVASSPLTRSSHHAGEDFAKLKAAREALYASRAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Brucella suis biovar 1 (strain 1330)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.957 kDa
Sequence
MVTVLNTVNQSGRLRHPEKAHRPDNEVLKKPDWIRVKAPVSRGYGETREIVRSNKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNISTGIPNALDPNEPENIAKAVKQMGLTHVVITSVDRDDLADGGAHHFAEVIKAVREAAPATTIEILTPDFLRKEGALEIVVKARPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVKPDEFKSFETIGKTKGFLLVASSPLTRSSHHAGEDFAKLKAAREALYASRAS

Gene
lipA
Protein
Lipoyl synthase
Organism
Neisseria meningitidis serogroup C (strain 053442)
Length
322 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.667 kDa
Sequence
MSEIKTDDPKRGIKLRGADKTARIPIKVVPLQEKLKKPEWIRAKLPSRKFFEIKDILREQKMHTVCEEASCPNIGECFSKGTATFMIMGDICTRRCPFCDVGHGRPNMLDPDEPRNLAESVKAMNLRYVVITSVDRDDLRDGGAQHFADCIKAIRETSPNTKIEILVPDFRGRLDIALKILAETPPDVMNHNLETHPSLYRKARPGANYQHSLDLLKRYKEMMPHIPTKSGIMVGLGETDEDVREIMRDMRAHNIEMITIGQYLQPSDGHLPVLRYVTPEQFKIFEKEAYELGFSNAAIGAMVRSSYHADEQAAEALRECEF

Gene
lipA
Protein
Lipoyl synthase
Organism
Klebsiella pneumoniae (strain 342)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.091 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSSRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPQKLAQTIADMGLRYVVVTSVDRDDLRDGGAQHFADCISAIREKNPSIKIETLVPDFRGRMDRALDILTVTPPDVFNHNLENVPRLYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNDEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFEEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.091 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSSRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPQKLAQTIADMGLRYVVVTSVDRDDLRDGGAQHFADCISAIREKNPSIKIETLVPDFRGRMDRALDILTVTPPDVFNHNLENVPRLYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNDEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFEEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.468 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPIKNMPTEQKEVLRKPEWMKIKLPADSQRIQDIKAAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPNAPEAEEPKKLAQTIHDMKLKYVVITSVDRDDLRDGGAQHFADCNREIRALNPHIKIETLVPDFRGRMEVALEALKDNPPDVFNHNLETAPRLYRKVRPGANYKWSLELLRQFKEQHPHVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEIALELGFTHAACGPFVRSSYHADLQAKGLEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.433 kDa
Sequence
MSKPIQMEKGVKYRDADKMALIPVKNMPSEQKEVLRKPDWMKIKLPADSQRIQDIKSAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLPVEAEEPKKLAKTIADMKLKYVVITSVDRDDLRDGGAEHFANCNREIRELNPHIKIETLVPDFRGRMDVALDLMKDNPPDVFNHNLETAPRLYRKARPGANYKWSLQLLQKFKEQHPNVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPSEFDELKEIALELGFTHAACGPFVRSSYHADMQAQGIEIK

Gene
lipA
Protein
Lipoyl synthase
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.454 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPIKNMPTEQKEVLRKPEWMKIKLPADSQRIQDIKAAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPNAPEAEEPKKLAQTIHDMKLKYVVITSVDRDDLRDGGAQHFADCNREIRALNPHIKIETLVPDFRGRMEVALEALKDNPPDVFNHNLETAPRLYRKVRPGANYKWSLELLRQFKEQHPHVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEVALELGFTHAACGPFVRSSYHADLQAKGLEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Vibrio cholerae serotype O1 (strain M66-2)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.468 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPIKNMPTEQKEVLRKPEWMKIKLPADSQRIQDIKAAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPNAPEAEEPKKLAQTIHDMKLKYVVITSVDRDDLRDGGAQHFADCNREIRALNPHIKIETLVPDFRGRMEVALEALKDNPPDVFNHNLETAPRLYRKVRPGANYKWSLELLRQFKEQHPHVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEIALELGFTHAACGPFVRSSYHADLQAKGLEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.451 kDa
Sequence
MSKPIQMEKGVKYRDADKMALIPVKNMPTEQKEVLRKPDWMKIKLPADSQRIQDIKAAMRKNKLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLPPEAEEPQKLARTIADMKLKYVVITSVDRDDLRDGGAQHFADCNREIRELNPDIKIETLVPDFRGRMDVALDLMKDNPPDVFNHNLETAPRLYRKARPGANYKWSLELLKKFKEQHPDVPTKSGLMMGLGETKEEIIEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPSEFDELKEVALELGFTHAACGPFVRSSYHADMQAQGLEIK

Gene
lipA
Protein
Lipoyl synthase
Organism
Vibrio tasmaniensis (strain LGP32)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.548 kDa
Sequence
MSKPIQMEKGVKYRDADKMALIPVKNMPAEQKEVLRKPAWMKIKLPSDSHRIQEIKSAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPNAPEAEEPKKLAKTIKDMKLKYVVITSVDRDDLRDGGAQHFADCNREIREQNPNIRIETLVPDFRGRMDVALELMKDNPPDVFNHNLETAPRLYRKARPGANYKWSLDLLRKFKEQHPNIPTKSGVMMGLGETKEEIVQVLKDLREHGVTMLTLGQYLAPSRHHLPVERYVPPSEFDELKEIALELGFTHAACGPFVRSSYHADLQAQGMEIK

Gene
lipA
Protein
Lipoyl synthase
Organism
Vibrio vulnificus (strain CMCP6)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.316 kDa
Sequence
MSKPIQMEKGVKYRDADKMALIPVKNMPTEQKEVLRKPDWMKIKLPADSQRIQDIKSAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLPPEAEEPTKLAKTIADMKLKYVVITSVDRDDLRDGGAKHFADCNREIRAQSPHIRIETLVPDFRGRMDVALEALKDNPPDVFNHNLETAPRLYRKVRPGANYQWSLDLLKKFKEQHPDVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEIALELGFTHAACGPFVRSSYHADMQAQGLEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Vibrio vulnificus (strain YJ016)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.316 kDa
Sequence
MSKPIQMEKGVKYRDADKMALIPVKNMPTEQKEVLRKPDWMKIKLPADSQRIQDIKSAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLPPEAEEPTKLAKTIADMKLKYVVITSVDRDDLRDGGAKHFADCNREIRAQSPHIRIETLVPDFRGRMDVALEALKDNPPDVFNHNLETAPRLYRKVRPGANYQWSLDLLKKFKEQHPDVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEIALELGFTHAACGPFVRSSYHADMQAQGLEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella piezotolerans (strain WP3 / JCM 13877)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.38 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKVVPSERDTMLRKPDWLRVKLPASNQRITEIKQALRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPKKLAQTIKDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRLLNPEIKIETLVPDFRGRIDKALDILAIEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKKFKERHPDIPTKSGLMMGLGESNEEIAQVLHDLRAHDVEMLTLGQYLQPSKFHLPVERYVSPAEFDELKDLAESIGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella sp. (strain ANA-3)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.465 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKIVPSERETMLRKPDWLRVKLPASNQRILEIKQALRSNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPEIKIEILVPDFRGRIDAALDILSTEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNEEIAQVLRDLREHKVEMLTLGQYLQPSKFHLPVERYVSPAEFDELKVLADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella sediminis (strain HAW-EB3)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.437 kDa
Sequence
MSRPERLQPGVKLRDADKVARIPVKVVPSERETMLRKPDWLRVKLPASSQRIDDIKKALRKNELHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDANEPKKMAQTIKDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRLLNPSIKIEILVPDFRGRIDAALDILATEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKKFKERHPDIPTKSGLMMGLGETNDQIAEVLKDLRAHNVEMLTLGQYLQPSKFHLRVERYVPPAEFDELREFAESIGFTHAACGPMVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella sp. (strain MR-4)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.465 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKIVPSERETMLRKPDWLRVKLPASNQRILEIKQALRSNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPEIKIEILVPDFRGRIDAALDILSTEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNEEIAQVLRDLREHKVEMLTLGQYLQPSKFHLPVERYVSPAEFDELKVLADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella sp. (strain MR-7)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.451 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKIVPSERETMLRKPDWLRVKLPASNQRILEIKQALRSNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDADEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPEIKIEILVPDFRGRIDAALDILSTEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNEEIAQVLRDLREHKVEMLTLGQYLQPSKFHLPVERYVSPAEFDELKVLADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella sp. (strain W3-18-1)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.345 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKIVPSERDTMLRKPDWLRVKLPASNQRILDIKQALRSNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPAIKIEILVPDFRGRIDAALDILATEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNEEIAQVLRDLREHKVEMLTLGQYLQPSKFHLPVERYVPPAEFDELKALADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella woodyi (strain ATCC 51908 / MS32)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.349 kDa
Sequence
MSRPERLQPGVKLRDADKVSRIPVKVVPSERETMLRKPDWLRVKLPSSSQRIDEIKQALRSNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAQEPKKLAQTIKDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRLLNPEIKIETLVPDFRGRIDAALDILATEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKKFKERHPDVPTKSGLMMGLGETNEEIAQVLKDLRAHNVEMLTLGQYLQPSKFHLPVERYVPPAEFDELRVFAEEIGFTHAACGPMVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.084 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVAIEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shigella boydii serotype 4 (strain Sb227)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shigella flexneri serotype 5b (strain 8401)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shigella flexneri
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shigella sonnei (strain Ss046)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Sodalis glossinidius (strain morsitans)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.981 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPIKTVAVERQEILRKPSWMKIKLPADSTRIQGIKVAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIADMGLRYVVVTSVDRDDLRDGGAQHFADCISAIRAKNPNIRIETLVPDFRGRMDRALEIINAAPPDVFNHNLENVPRLYRQVRPGADYHWSLKLLENFKVANPQLPTKSGLMVGLGETNAEIVDVMRDLCRHGVTMLTLGQYLQPSRHHLPVKRYVSPQEFDEMKQEALAMGFTHAACGPFVRSSYHADLQAKGIEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Cronobacter sakazakii (strain ATCC BAA-894)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.961 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPSIKIETLVPDFRGRMDRALEILTATPPDVFNHNLENVPRLYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRAHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFEEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGEEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella paratyphi A (strain AKU_12601)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella schwarzengrund (strain CVM19633)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella typhi
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.998 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPCVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Serratia proteamaculans (strain 568)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.157 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKTVVTERQELLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPEKLAQTIADMGLRYVVITSVDRDDLRDGGAQHFADCIAAIRAKNPTIKIETLVPDFRGRMDRALEILTETPPDVFNHNLENVPRVYRQVRPGANYEWSLKLLERFKEAHPHIPTKSGLMVGLGETNAEIVEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKEEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.332 kDa
Sequence
MNRPERLQPGVKLRDADKVARIPVKIMPSERETMLRKPDWLRVKLPASNQRITEIKQALRSNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDADEPVKLAKTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRALNPHIQIETLVPDFRGRIDVALDILSTNPPDVFNHNLETAPAHYRKARPGANYQWSLDLLKRFKERHPNIPTKSGLMMGLGETNEEIIQVLKDLRAHDVNMLTLGQYLQPSKFHLPVERYVSPQEFDELKVIAEDLGFSHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella baltica (strain OS223)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.376 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKIVPSERDTMLRKPDWLRVKLPASNQRILEIKQALRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPDIKIETLVPDFRGRIDAALDILSTEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNEEIAQVLRDLRAHNVEMLTLGQYLQPSKFHLPVERYVPPAEFDELKALADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella baltica (strain OS155 / ATCC BAA-1091)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.376 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKIVPSERDTMLRKPDWLRVKLPASNQRILEIKQALRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPDIKIETLVPDFRGRIDAALDILSTEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNEEIAQVLRDLRAHNVEMLTLGQYLQPSKFHLPVERYVPPAEFDELKALADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella baltica (strain OS185)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.376 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKIVPSERDTMLRKPDWLRVKLPASNQRILEIKQALRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPDIKIETLVPDFRGRIDAALDILSTEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNDEIAQVLRDLRAHKVEMLTLGQYLQPSKFHLPVERYVPPAEFDELKALADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella baltica (strain OS195)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.376 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKIVPSERDTMLRKPDWLRVKLPASNQRILEIKQALRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPDIKIETLVPDFRGRIDAALDILSTEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNEEIAQVLRDLRAHNVEMLTLGQYLQPSKFHLPVERYVPPAEFDELKALADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.313 kDa
Sequence
MNRPERLQPGVKLRDADKVARIPVKIVPSERETMLRKPDWLRVKLPASNQRILEIKAALRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPDIKIETLVPDFRGRIDAALDILSAEPPDVFNHNLETAPAHYRKARPGANYQWSLDLLKRFKERHPHIPTKSGLMMGLGETNEEIAEVLRDLRSHNVEMLTLGQYLQPSKFHLPVVRYVPPAEFDELKVLADELGFTHAACGPMVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella frigidimarina (strain NCIMB 400)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.205 kDa
Sequence
MNRPERLQPGVKLRDADKVARIPVKVVPSERETMLRKPDWLRVKLPSSNQRILEIKAALRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKADADEPKKLAQTIKDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRLLNPEIKIETLVPDFRGRIDAALDILATEPPDVFNHNLETAPAHYRKARPGANYQWSLDLLKRFKERHPTIPTKSGLMMGLGETNEEIAEVLRDLRAHNVEMLTLGQYLQPSKFHLPVERYVPPAEFDELKALADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella halifaxensis (strain HAW-EB4)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.366 kDa
Sequence
MNRPERLQPGVKLRDAEKVSRIPVKVVPSERETMLRKPDWLRVKLPASNQRITDIKQALRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPKKLAQTIKDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRLLNPEIKIETLVPDFRGRIDAALDILATEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKKFKERHPDIPTKSGLMMGLGESNEEIAQVLYDLRAHNVEMLTLGQYLQPSKFHLAVERYVSPAEFDELKELAESIGFTHAACGPLVRSSYHADLQAQGKEVR

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.45 kDa
Sequence
MSRPERLQPGVKLRDADKVSRIPVKVVPSERETMLRKPDWLRVKLPASNQRIVDIKQALRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPEIKIEILVPDFRGRIDAALEILATEPPDVFNHNLETAPKHYRKARPGANYQWSLDLLKKFKEQHPHIPTKSGLMMGLGETNEEIAEVLRDLRAHNVEMLTLGQYLQPSKFHLPVERYVPPAEFDELKDYAEEIGFTHAACGPMVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella oneidensis (strain MR-1)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.464 kDa
Sequence
MNRPERLQPGVKLRDAEKVSRIPVKIVPSERETMLRKPDWLRVKLPASNQRILDIKQALRANGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDEQEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPEIKIEILVPDFRGRIDAALDILSTEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNDEIAQVLRDLREHKVEMLTLGQYLQPSKFHLPVERYVSPAEFDELKALADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.337 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKVVPSERDTMLRKPDWLRVKLPASNQRITDIKQALRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPKKLAQTIKDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRLLNPEIKIETLVPDFRGRIDAALEILATEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKKFKERHPNIPTKSGLMMGLGETNEEIAQVLHDLRAHNVEMLTLGQYLQPSKFHLPVERYVSPAEFDELKELAESIGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.345 kDa
Sequence
MNRPERLQPGVKLRDADKVSRIPVKIVPSERDTMLRKPDWLRVKLPASNQRILDIKQALRSNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKPDAEEPVKLAQTIRDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRKLNPAIKIEILVPDFRGRIDAALDILATEPPDVFNHNLETAPMHYRKARPGANYQWSLDLLKRFKERHPNVPTKSGLMMGLGETNEEIAQVLRDLREHKVEMLTLGQYLQPSKFHLPVERYVPPAEFDELKALADELGFTHAACGPLVRSSYHADLQAQGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.046 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDTNEPLKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPAIKIETLVPDFRGRMDRALEILNATPPDVFNHNLENVPRVYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEAMAMGFTHAACGPFVRSSYHADMQAKGLEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.215 kDa
Sequence
MRHRWEDRPVAPPPDGRPTEYLPFRQERGRHGRPGWLKARVPDGPGYREIKETMRGLSLHTVCEEARCPNIGECWNNRTATFMILGNVCTRSCGFCAVLTGRPQELDLEEPYRVADAVKKMGLRHAVITSVNRDELPDGGASVFAATIRAIRREVPGCAVEVLTPDFKGDRDAIKTVIDARPDTFNHNIETVPRLYPAVRPQAKYGRSLEVLRYAKELDPGVLTKSGFMVGLGEVEEEIVRTMRDLREHGVDILTIGQYLRPTENHLPMARYYTPQEFARYKKLGLEMGFSHVESGPLVRSSYHAHEQTEDARRGALGARG

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella agona (strain SL483)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.07 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVITERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALEILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella choleraesuis (strain SC-B67)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella dublin (strain CT_02021853)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella enteritidis PT4 (strain P125109)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella heidelberg (strain SL476)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella newport (strain SL254)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Salmonella paratyphi C (strain RKS4594)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.042 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTERDALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDAEEPQKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIRAKSPEIKIETLVPDFRGRMDRALDILNATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O9:H4 (strain HS)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O1:K1 / APEC
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli (strain K12)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. Free octanoate is not a substrate for LipA.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli (strain SE11)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli (strain UTI89 / UPEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Edwardsiella ictaluri (strain 93-146)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.254 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKSVAVEREQLLRKPEWMKIKLPADSSRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLAPDTNEPEKLAQTIADMGLRYVVITSVDRDDLRDGGAQHFADCIHAIRAKSPQIRIETLVPDFRGRMDRALEILHDNPPDVFNHNLENIPRLYRQVRPGANYEWSLRLLQQFKQQHPQIPTKSGLMVGLGETNQEIIEVMRDLRAHGVTMLTLGQYLQPSRHHLPVQRYVSPEEFAEMKAEALAMGFTHAACGPFVRSSYHADLQAQGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Enterobacter sp. (strain 638)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.029 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTEREALLRKPEWMKIKLPADSSRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPLKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCISAIREKSPSIKIETLVPDFRGRMDRALEILTATPPDVFNHNLENVPRVYRQVRPGADYNWSLKLLERFKEAHPHIPTKSGLMVGLGETNAEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEAMAMGFTHAACGPFVRSSYHADMQAKGEEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.939 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKTVVTERTEVLRKPEWMKIKLPADSSRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPTTPDANEPGKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCISAIREKSPTIKIETLVPDFRGRMDRALEILNATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPEIPTKSGLMVGLGETNAEIVEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAAAMDMGFTHAACGPFVRSSYHADMQAKGLEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.055 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVVTEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPSIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFEEMKAEALAMGFTHAACGPFVRSSYHADLQAKGIEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.298 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKTVMTERTEILRKPEWMKIKLPADSSRIQGIKSAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPMAPDTNEPVKLAQTIKDMALRYVVITSVDRDDLRDGGAQHFADCISAIREKNPSIKIETLVPDFRGRMDRALEILTATPPDVFNHNLENVPRVYRQVRPGANYEWSLKLLEKFKEAHPDIPTKSGLMVGLGETNEEILDVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPQEFDEMKEEALAMGFTHAACGPFVRSSYHADLQAKGEEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.118 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPIKTVVTERQELLRKPEWMKIKLPADSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIKDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTVTPPDVFNHNLENVPRVYRQVRPGANYEWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGLEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.086 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKNVVTERQELLRKPEWLKIKLPTDSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIQDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMHDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.086 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKNVVTERQELLRKPEWLKIKLPTDSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIQDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMHDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Proteus mirabilis (strain HI4320)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.33 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKTIVTEREELLRKPEWMKIKLPADSSKIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPNAPDPQEPIKLAQTIKDMGLRYVVITSVDRDDLRDGGAQHFADCITAIREKNPNIRIETLVPDFRGRMDKALEILTDTPPDVFNHNLENVPRVYRQVRPGANYQWSLTLLERFKQAHPNIPTKSGLMVGLGETNEEIIDVMRDLRKHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFEYMKEQALAMGFTHAACGPFVRSSYHADLQAQGIEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudoalteromonas haloplanktis (strain TAC 125)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.257 kDa
Sequence
MNKPVKMEPGVKLRDAAKMALIPVKVLPTEKNEMLRKPEWLKIRLPKSTERIEGIKQAMRKHGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPLTPDATEPEKLALTIKDMKLSYVVITSVDRDDLRDGGAQHFADCIREIRKHSPNITIEILVPDFRGRMDRALEILIETPPDVFNHNLETAPRLYKLARPGADYKWSLELLRRFKEAHPEIKTKSGLMVGLGEEISEIEEVLRDLRAHNVDMLTVGQYLQPSKHHLPVKRYVPPAEFDALKAYADEIGFTHAASGPFVRSSYHADQQAAGKEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.489 kDa
Sequence
MSKPVRMEPGVKLRDGDKMALIPVKFMPDPNEEVLRKPDWMRIKLPPSSQKIEHIKSTLRKNKLHSVCEEASCPNLAECFNHGTATFMIMGAICTRRCPFCDVAHGRPLALDPDEPKKLALTIKEMGLKYVVITSVDRDDLRDGGAQHFADCIKQIREHSPQTRIEILTPDFRGRMEQALEVFRETPPDVFNHNLETAPRMYRVARPGADYKWSLELLRRIKEMHPHVPTKSGVMMGLGETNEEIVQVLKDLREHGVNMLTLGQYLQPSRHHLPVKRYVPPAEFDELKDVAMGLGFSHAACGPFVRSSYHADLQAKGEEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.394 kDa
Sequence
MSKPIQMEKGVKYRDADKMALIPVKNMPTEQKEVLRKPEWMKIKLPASSKRIDDIKSAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPEAEEPKKLAKTIQDMKLKYVVITSVDRDDLRDGGAQHFADCNREIRALNPEIRIETLVPDFRGRMDRALEAMIDNPPDVFNHNLETAPRLYRKVRPGANYQWSLDLLKKFKEQHPNVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEIALELGFTHAACGPFVRSSYHADLQAKGEEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Aliivibrio fischeri (strain MJ11)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.38 kDa
Sequence
MSKPIQMEKGVKYRDADKMALIPVKNMPTEQKEVLRKPEWMKIKLPASSKRIDDIKSAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPEAEEPKKLAKTIQDMKLKYVVITSVDRDDLRDGGAQHFADCNREIRALNPEIRIETLVPDFRGRMDRALEAMIDNPPDVFNHNLETAPRLYRKVRPGANYQWSLDLLKKFKDQHPNVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEIALELGFTHAACGPFVRSSYHADLQAKGEEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Aliivibrio salmonicida (strain LFI1238)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.437 kDa
Sequence
MSKPIQMEKGVKYRDADKMALIPVKNMPTEKKEVLRKPEWMKIKLPSSSKRIDEIKSAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPEAEEPKKLAKTIKDMKLKYVVITSVDRDDLRDGGAQHFADCNREIRELNPEIRIETLVPDFRGRMDRALDAMHSNPPDVFNHNLETAPRLYRKVRPGANYQWSLDLLKKFKEQHPTVPTKSGVMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKVIALELGFTHAACGPFVRSSYHADLQAKGEEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli (strain 55989 / EAEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O157:H7
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O81 (strain ED1a)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli O8 (strain IAI1)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.072 kDa
Sequence
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.956 kDa
Sequence
MVTVLDLVNQGKRERHPEKAHRPDNVVLKKPEWIRVKAPVSRGYSETRDIVRSNKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNVSTGIPTALDPNEPENVAKAVKQMGLTHVVITSVDRDDLADGGAQHFAEVIQAIREATPATTIEILTPDFLRKEGALEVVVRARPDVFNHNLETVPSRYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVTPDEFKSFETIGRTKGFLLVASSPLTRSSHHAGDDFAKLRAAREAQISARA

Gene
lipA
Protein
Lipoyl synthase
Organism
Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.74 kDa
Sequence
MVTILDTLKPGAAKPRHPEKAHRPDTPVLRKPEWIRVKAPGSAVYAETKQIVRENKLVTVCEEAGCPNIGECWTKKHATMMIMGDTCTRACSFCNVKTGLPAPLDVDEPENVANAVAKLGLRHVVITSVDRDDLADGGAAHFVEVIEAIRRRSPGTTIEILTPDFLRKDGALEKVVAARPDVFNHNLETVPRLYLNIRPGARYFHSLRLLQRVKEIDPTIFTKSGIMVGLGETREEVLQVMDDMRSAQIDFLTIGQYLQPTRKHAAIDRFVTPDEFKSYETIARSKGFLLVSASPLTRSSYHADEDFARLRDARSSALSRG

Gene
lipA
Protein
Lipoyl synthase
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.247 kDa
Sequence
MSKPIQIERGVKYRDADKMALIPVRTVVTERQELLRKPEWMKIKLPADSSRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLTPDANEPEKLAQTIHDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRRKNPHIRIETLVPDFRGRMDRALEILTATPPDVFNHNLENVPRVYRQVRPGANYEWSLKLLENFKNAHPDITTKSGLMVGLGETNAEIVEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGIEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.188 kDa
Sequence
MSKPIQIERGVKYRDADKMALIPVRTVVTERQEILRKPEWMKIKLPADSSRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLTPDANEPEKLAQTIHDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRRKNPNIRIETLVPDFRGRMDRALEILTATPPDVFNHNLENVPRVYRQVRPGANYEWSLKLLENFKNAHPDIPTKSGLMVGLGETNAEIVDVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEAIAMGFTHAACGPFVRSSYHADLQAKGIEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Tolumonas auensis (strain DSM 9187 / TA4)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.198 kDa
Sequence
MTKPITVQPGVQLRDADKMALIPVKFLPEQEGEQLKKPDWMRIRLPKTDEKIQNVKNIMRKNNLHSVCEEASCPNLSECFNHGTATFMILGAICTRHCPFCDVAHGKPLAPDADEPKKLANTIREMALKYVVITSVDRDDLRDGGAQHFADCIREIRLASPNTRIETLTPDFRGRMDKALDVFRETPPDVFNHNLETAPRLYSMARPGADYAWSLKLLQKMKELHPDLPTKSGLMMGLGETNDEIVQVLKDLRAHGVTMLTLGQYLQPSRHHLPVKRYVPPQEFDELKAIALDLGFTHAACGPFVRSSYHADLQAQGQEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.684 kDa
Sequence
MVTVLDAIANAPRLRHPEKAHKPDQEVLRKPDWIRVKAPVSKGYAETREIVKSHKLVTVCEEAGCPNIGECWEKKHATFMIMGEICTRACAFCNVATGIPTALDPDEPARVAHAVKQMGLSHVVITSVDRDDLADGGAQHFADVIRAIRAATPSTTIEILTPDFLRKDGALEIVVAARPDVFNHNLETVPSNYLKVRPGARYFHSIRLLQRVKELDPSIFTKSGIMVGLGEERNEILQLMDDLRSANVDFMTIGQYLQPSKKHHPVIRFVTPEEFKSFETIGRTKGFLLVASSPLTRSSHHAGDDFARLRAAREAQLQKSV

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.086 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKNVVTERQELLRKPEWLKIKLPTDSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIQDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMHDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia pestis
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.086 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKNVVTERQELLRKPEWLKIKLPTDSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIQDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMHDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.086 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKNVVTERQELLRKPEWLKIKLPTDSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIQDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMHDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia pestis bv. Antiqua (strain Nepal516)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.086 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKNVVTERQELLRKPEWLKIKLPTDSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIQDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMHDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia pestis (strain Pestoides F)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.086 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKNVVTERQELLRKPEWLKIKLPTDSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIQDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMHDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.086 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKNVVTERQELLRKPEWLKIKLPTDSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIQDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMHDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
Length
321 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.086 kDa
Sequence
MSKPIQMERGVKYRDADKMALIPVKNVVTERQELLRKPEWLKIKLPTDSSRIQGIKAAMRKNGLHSVCEEASCPNLSECFNHGTATFMILGAICTRRCPFCDVAHGRPVTPDANEPEKLAQTIQDMGLRYVVITSVDRDDLRDGGAQHFADCISAIRAKNPTIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRVYRQVRPGANYDWSLKLLERFKEAHPDIPTKSGLMVGLGETNAEIVEVMHDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPAEFDEMKAEAMAMGFTHAACGPFVRSSYHADLQAKGMEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.202 kDa
Sequence
MVTVVDRVTDRRLRHPEKAHRPDTSVQKKPDWIRVKAPTSQVYKETHGIVRAHKLVTVCEEAGCPNIGECWSQRHASFMILGEICTRACAFCNVATGIPFAVDENEPERVADAVARMELKHVVITSVDRDDLADGGAEHFAKVIYAIRRKAPKTTIEVLTPDFRHKDGALEIVVAAKPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVPPEEFESFAKIGKVKGFLHMASNPLTRSSHHAGDDFAILQKARDEKFALQR

Gene
lipA
Protein
Lipoyl synthase
Organism
Bartonella quintana (strain Toulouse)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.303 kDa
Sequence
MVTVVDRVTSRRLRHPEKMHRPDTSIQKKPDWIRVKAPTSKIYKETYDIVRAHKLVTVCEEAGCPNVGECWSQRHASFMILGEICTRACAFCNVATGIPLAVDDNEPERVADAVAQMELKHVVITSVDRDDLADGGAQHFAKVIYAIRRKAPKTTIEVLTPDFRHKDGALEIVVAAKPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFFPPEEFESFAKIGKVKGFLHMASNPLTRSSHHAGDDFAILQKARDEKFALQR

Gene
lipA
Protein
Lipoyl synthase
Organism
Bartonella tribocorum (strain CIP 105476 / IBS 506)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.153 kDa
Sequence
MVTVVDRVTNRRLRHPEKAHRPDTSVQKKPDWIRVKAPTSPVYKETHGIVRTHKLVTVCEEAGCPNIGECWSQRHASFMILGEICTRACAFCNVATGIPLAVDDDEPERVADAVARMELKHVVITSVDRDDLADGGAEHFAKVIYAIRRKAPKTTIEVLTPDFRHKDGALEVVVAAKPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRTADVDFMTIGQYLQPTRKHHPVIRFVPPEEFESFAKIGKVKGFLHMASNPLTRSSHHAGDDFAILQKARDEKFALQR

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.492 kDa
Sequence
MIGKLVRDLKIPDQRHPEKAHRPDNVQPKKPSWIRVKAPTSEGYKETRDIIRGQKLATVCEEAGCPNVGECWSQGHATMMIMGEICTRGCSFCNVATGRPQALDAFEPGRVAHAVSQLGLKHVVVTSVDRDDLEDGGAEHFAQTIRAIRHRAPATTIEVLVPDFLKCGPSALETVVAARPDVFNHNLETVPGLYPEVRPGARYFHSLRLLQRAKELDPSIFTKSGIMVGLGEDRQGVLQVMDDMRSAEVDFLTIGQYLQPTPKHHRVDRFVTPEEFAGYEKAAYGKGFLMVSATPLTRSSYHAGDDFARLRDARQKRLGA

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.492 kDa
Sequence
MIGKLVRDLKIPDQRHPEKAHRPDNVQPKKPSWIRVKAPTSEGYKETRDIIRGQKLATVCEEAGCPNVGECWSQGHATMMIMGEICTRGCSFCNVATGRPQALDAFEPGRVAHAVSQLGLKHVVVTSVDRDDLEDGGAEHFAQTIRAIRHRAPATTIEVLVPDFLKCGPSALETVVAARPDVFNHNLETVPGLYPEVRPGARYFHSLRLLQRAKELDPSIFTKSGIMVGLGEDRQGVLQVMDDMRSAEVDFLTIGQYLQPTPKHHRVDRFVTPEEFAGYEKAAYGKGFLMVSATPLTRSSYHAGDDFARLRDARQKRLGA

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.494 kDa
Sequence
MIGKLVRDLKIPDQRHPEKAHRPDNDQPRKPSWIRVKAPTSEGYKETRDIIRGQKLATVCEEAGCPNVGECWGQGHATMMIMGEICTRGCTFCNVATGKPQALDAFEPGRVAHAVSQLGLKHVVVTSVDRDDLEDGGAEHFAQTIRAIRHRAQGTTVEVLVPDFLKCGPEALETVVAARPDVFNHNLETVPGLYPEVRPGARYFHSLRLLQRAKELDPQIFTKSGIMVGLGEDRQGVMQVMDDMRAAGVDFLTIGQYLQPTPKHHRVDRFVTPEEFASYEKAAYGKGFLMVSATPLTRSSYHAGEDFARLRAARLERLGA

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodobacter sphaeroides (strain KD131 / KCTC 12085)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.492 kDa
Sequence
MIGKLVRDLKIPDQRHPEKAHRPDNVQPKKPSWIRVKAPTSEGYKETRDIIRGQKLATVCEEAGCPNVGECWSQGHATMMIMGEICTRGCSFCNVATGRPQALDAFEPGRVAHAVSQLGLKHVVVTSVDRDDLEDGGAEHFAQTIRAIRHRAPATTIEVLVPDFLKCGPSALETVVAARPDVFNHNLETVPGLYPEVRPGARYFHSLRLLQRAKELDPSIFTKSGIMVGLGEDRQGVLQVMDDMRSAEVDFLTIGQYLQPTPKHHRVDRFVTPEEFAGYEKAAYGKGFLMVSATPLTRSSYHAGDDFARLRDARQKRLGA

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidiphilium cryptum (strain JF-5)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.05 kDa
Sequence
MRVEIDHRNSGGGKLRHPEKQHRPDNPIQRKPAWIRVKAPNHPVYHETRALMREAKLVTVCEEAACPNIGECWSQRHATMMIMGEICTRACAFCNVTTGQPAPLAADEPARVAEAVARLGLQHVVITSVDRDDLDDGGAAHFAAVIGAIRAAAPSTTIEILTPDFLRKPGALEVVVAARPDVFNHNLETVPRLYPSIRPGARYYQSLRLLDRVKQLDPSIFTKSGLMAGLGEDRGEVGQVMDDLRIADVDFLTIGQYLQPTVKHAAVDRFVTPDEFADLAAMARAKGFLMVSATPLTRSSYHADADFAALREARAARHAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Mannheimia succiniciproducens (strain MBEL55E)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.221 kDa
Sequence
MSTAFKMERGVKYRDAAKTSIIQVKNIDPDQELLQKPSWMKIKLPANSAKIQSIKNGMRRHGLNSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPEEPKKLAETIQDMKLKYVVITSVDRDDLPDRGAGHFAECIKEIRKINPNTQIEILVPDFRGRIEQALDKLKDNPPDVFNHNLENVPRLYRDIRPGADYQWSLKLLREFKALFPHIPTKSGLMVGLGETNEEILNVMQDLRNNGVTMLTLGQYLQPSRFHLPVARYVPPEEFDEFRTKAEVMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.337 kDa
Sequence
MAVVLDLLANDARPRHPEKAHRPDQPIQRKPDWIRVRAPGSPGWAETNRIVREHGLVTVCEEAGCPNIGECWEKKHATFMIMGDTCTRACAFCNVRTGLPQGLDGDEPARVADAVARLGLSHVVITSVDRDDLRDGGAGHFAAVIGAIRQASPGTTIEVLTPDFLRKEGALDVVVAAKPDVFNHNLETVPSKYLTVRPGARYFHSVRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRSAEVDFLTIGQYLQPTKKHHPVKRFVPPDEFRAYETTAYAKGFLLVSATPLTRSSHHAGADFARLKQARLDRLATA

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidiphilium cryptum (strain JF-5)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.05 kDa
Sequence
MRVEIDHRNSGGGKLRHPEKQHRPDNPIQRKPAWIRVKAPNHPVYHETRALMREAKLVTVCEEAACPNIGECWSQRHATMMIMGEICTRACAFCNVTTGQPAPLAADEPARVAEAVARLGLQHVVITSVDRDDLDDGGAAHFAAVIGAIRAAAPSTTIEILTPDFLRKPGALEVVVAARPDVFNHNLETVPRLYPSIRPGARYYQSLRLLDRVKQLDPSIFTKSGLMAGLGEDRGEVGQVMDDLRIADVDFLTIGQYLQPTVKHAAVDRFVTPDEFADLAAMARAKGFLMVSATPLTRSSYHADADFAALREARAARHAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Mannheimia succiniciproducens (strain MBEL55E)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.221 kDa
Sequence
MSTAFKMERGVKYRDAAKTSIIQVKNIDPDQELLQKPSWMKIKLPANSAKIQSIKNGMRRHGLNSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPEEPKKLAETIQDMKLKYVVITSVDRDDLPDRGAGHFAECIKEIRKINPNTQIEILVPDFRGRIEQALDKLKDNPPDVFNHNLENVPRLYRDIRPGADYQWSLKLLREFKALFPHIPTKSGLMVGLGETNEEILNVMQDLRNNGVTMLTLGQYLQPSRFHLPVARYVPPEEFDEFRTKAEVMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.337 kDa
Sequence
MAVVLDLLANDARPRHPEKAHRPDQPIQRKPDWIRVRAPGSPGWAETNRIVREHGLVTVCEEAGCPNIGECWEKKHATFMIMGDTCTRACAFCNVRTGLPQGLDGDEPARVADAVARLGLSHVVITSVDRDDLRDGGAGHFAAVIGAIRQASPGTTIEVLTPDFLRKEGALDVVVAAKPDVFNHNLETVPSKYLTVRPGARYFHSVRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRSAEVDFLTIGQYLQPTKKHHPVKRFVPPDEFRAYETTAYAKGFLLVSATPLTRSSHHAGADFARLKQARLDRLATA

Gene
lipA
Protein
Lipoyl synthase
Organism
Erythrobacter litoralis (strain HTCC2594)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.443 kDa
Sequence
MGGMNDLSSTPAPEGDRPARQRKPDWIRVKAPVSKGYHETRKLMRELNLNTVCEEAACPNIGECWTKKHATVMILGDVCTRACAFCNVKTGMPRIVDPMEPENTAIAAAKMGLQHIVITSVDRDDLPDGGAGQFVKVIEALRRETPDTTIEILTPDFRGKMRAAVEAICEAGPDVYNHNLETVPRLYPTIRPGARYYASLRLLEEVKSHDPMIFTKSGIMLGLGEQRLEVHQVMDDMRSADVDFITMGQYLQPTPKHAKVEDFVTPKAFDAFGAIARAKGFLQVASSPLTRSSYHAGDDFAEMRAAREAKLAKERERAQG

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.341 kDa
Sequence
MSNARPQAGEKLRDDEKVKHIPITIMPTEKAEMLRKPEWIKIRLPRTTDRIDHIKKTLRKNNLHSVCEEASCPNLAECFNHGTATFMILGDICTRRCPFCDVAHGKPLPPSAEEPVKLAKTIAEMQLKYVVITSVDRDDLRDGGAQHFVDCINAIREHSPTTKIEVLVPDFRGRMDKALEILKNGVPDVFNHNLETIPRLYRECRPGANYQWSLDLLKKFKEQHPDIPTKSGLMMGMGENKEEIAEVLKDLRAHNVEMLTLGQYLQPSKHHFPLKRYVHPTEFDELGVIAKEIGFTHAACGPMVRSSYHADKQAAGVEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / 130Z)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.292 kDa
Sequence
MGTPFKMERGVKYRDAAKTSIIKVTNIDPDRELLQKPSWMKIKLPASSAKIDSIKNGMRRHGLHSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPEEPRKLAETIQDMKLKYVVITSVDRDDLPDRGAGHFADCVREIRALNPEIKIEILVPDFRGRIELALEKLKNNPPDVFNHNLENIPRLYREIRPGADYEWSLKLLREFKAMFPHIPTKSGLMVGLGENNEEILQVMRDLRTNGVTMLTLGQYLQPSRYHLPVARYVSPEEFDEFREKAAEMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Pasteurella multocida (strain Pm70)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.349 kDa
Sequence
MGTPFKMERGVKYRDAAKTSIIPVKNIDPNQELLKKPEWMKIKLPANSAKIDSIKNGMRRHGLHSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPEEPRKLAETIQDMKLRYVVITSVDRDDLPDRGAGHFAECVKEIRQLNPNIKIEILVPDFRGRIEQALDKLKDNPPDVFNHNLENVPRLYREIRPGADYQWSLKLLKDFKAMFPHIPTKSGLMVGLGETNEEILQVMQDLRDHGVTMLTLGQYLQPSRHHLPVARYVPPAEFDEFRDKAQAMGFEHAACGPFVRSSYHADLQAKGEIVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.798 kDa
Sequence
MAEFRIDPEMELPVLPSRARADVSRKPEWLKINLRTDAEFVELKRLMRGQGLHTVCEEARCPNIFECWNRRTATFMILGDICTRNCGFCAVRSGVPTGLDLAEPERVADACVQLGLRHVVVTSVARDDLSDGGASIFAETIRAIRRKNPFTGVEVLIPDFGGNWDALAVVMDAEPDVLNHNIETVRRLSDRVRSRAKYDRSLELLRRAKEMKPHVSTKSSIMVGLGETMQELYEAMDDLRAAGVDIVTFGQYLRPTARHLAVEKFYTPAEFEHLREEALKRGFAHCESGPLVRSSYHADEQSAQAVARRTGAGRAAQTGD

Gene
lipA
Protein
Lipoyl synthase
Organism
Thioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.085 kDa
Sequence
MTDTRKSPEPGVKLRAADKVARIPVKIAPTEKPLRKPAWIRARTHGSPEVQRLKRVLREQRLHTVCEEASCPNLGECFGHGTATFMIMGDICTRRCPFCDVAHGRPEPLDAEEPENLARTIAAMGLRYVVITSVDRDDLRDGGARHFVDCIRTTRAHSPDIRIEILVPDFRGRMDVALAILNEAPPDVFNHNLETVPRLYREARPGSDYDWSLDLIQRFKETHPQVPTKSGLMLGLGEEMHEVEAVMRDLRDHGCDMLTLGQYLQPSLHHLPVKRYVTPEEFDRLAEIGYAMGFSQVASGPMVRSSYHADQQAQKVIPEG

Gene
lipA
Protein
Lipoyl synthase
Organism
Haemophilus influenzae (strain 86-028NP)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.211 kDa
Sequence
MSTPFKMERGVKYRDAAKTSIIPVKNIDPNQELLKKPEWMKIKLPASSAKIESIKNGMRRHGLHSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPEEPQKLAETIQDMKLKYVVITSVDRDDLPDRGAGHFSECVKAVRELNPNIKIEILVPDFRGRITQALEKLKDNPPDVFNHNLENVPRLYKEIRPGADYEWSLKLLREFKEIFPNIPTKSGLMVGLGETNEEILQVMQDLRDNGVTMLTLGQYLQPSRHHLPVARYVPPTEFDEFRDKANEMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Haemophilus influenzae (strain PittEE)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.129 kDa
Sequence
MSTPFKMERGVKYRDAAKTSIIPVKNIDPNQDLLKKPEWMKIKLPASSAKIESIKNGMRRHGLHSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPEEPQKLAETIQDMKLKYVVITSVDRDDLPDRGAGHFSECVKAVRELNPNIKIEILVPDFRGRVTQALEKLKDNPPDVFNHNLENVPRLYKEIRPGADYGWSLKLLREFKEMFPNIPTKSGLMVGLGETNEEILQVMQDLRDNGVTMLTLGQYLQPSRHHLPVARYVPPTEFDEFRDKANEMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Haemophilus influenzae (strain PittGG)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.199 kDa
Sequence
MSTPFKMERGVKYRDAAKTSIIPVKNIDPNQELLKKPEWMKIKLPASSAKIESIKNGMRRHGLHSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPEEPQKLAETIQDMKLKYVVITSVDRDDLPDRGAGHFSECVKAVRELNPNIKIEILVPDFRGRVTQALEKLKDNPPDVFNHNLENVPRLYKEIRPGADYEWSLKLLREFKEMFPNIPTKSGLMVGLGETNEEILQVMQDLRDNGVTMLTLGQYLQPSRHHLPVARYVPPTEFDIFRDKANEMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.197 kDa
Sequence
MSTPFKMERGVKYRDAAKTSIIPVKNIDPNQDLLKKPEWMKIKLPASSAKIESIKNGMRRHGLHSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPEEPQKLAETIQDMKLKYVVITSVDRDDLPDRGAGHFSECVKAVRELNPNIKIEILVPDFRGRITQALEKLKDNPPDVFNHNLENVPRLYKEIRPGADYEWSLKLLREFKEIFPNIPTKSGLMVGLGETNEEILQVMQDLRDNGVTMLTLGQYLQPSRHHLPVARYVPPTEFDEFRDKANEMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Haemophilus parasuis serovar 5 (strain SH0165)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.193 kDa
Sequence
MGTPFKMERGVKYRDAAKTSIIPVKNIDPNQELLKKPEWMKIKLPANSAKIESIKNGMRRHGLHSVCEEASCPNLHECFNHGTATFMIMGAICTRRCPFCDVAHGKPLPLDKDEPKKLAETIQDMKLKYVVITSVDRDDLPDRGAGHFAECVKEIRALNPGIKIEILVPDFRGRVEQAIEILKENPPDVFNHNLENVPRLYKEIRPGADYEWSLKLLKEFKAVFPDIPTKSGIMVGLGETNEEILQVMQDLRDHGVTMLTLGQYLQPSRHHLPVARYVHPTEFDMFREKANEMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Haemophilus somnus (strain 129Pt)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.285 kDa
Sequence
MTTPFKMERGVKYRDAAKTSIIPVKNIDPNQELLKKPEWMKIKLPANSAKINSIKNGMRRHGLHSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPDEPKKLAETIQDMKLRYVVITSVDRDDLPDRGAGHFAECVKEIRKLNPGIKIEILVPDFRGRIEQALEKLKDNPPDVFNHNLENVPRLYREIRPGADYNWSLKLLKEFKTIFPHIPTKSGIMVGLGETNEEILQVMQDLRDNGVTMLTLGQYLQPSRHHLPVARYVPPEEFDDFRDKAEKMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Histophilus somni (strain 2336)
Length
320 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.285 kDa
Sequence
MTTPFKMERGVKYRDAAKTSIIPVKNIDPNQELLKKPEWMKIKLPANSAKINSIKNGMRRHGLHSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLPPDPDEPKKLAETIQDMKLRYVVITSVDRDDLPDRGAGHFAECVKEIRKLNPGIKIEILVPDFRGRIEQALEKLKDNPPDVFNHNLENVPRLYREIRPGADYNWSLKLLKEFKTIFPHIPTKSGIMVGLGETNEEILQVMQDLRDNGVTMLTLGQYLQPSRHHLPVARYVPPEEFDDFRDKAEKMGFEHAACGPFVRSSYHADLQASGGLVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.018 kDa
Sequence
MVTIVDTLSNTPLRPRHPEKANRPDSISPAKPSWIRVKAPTTRGYADTRNIVRENGLVTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVKTGLPAALDAGEPEHVAEATFKLGLAHVVVTSVDRDDLADGGAAHIAATIRAIRATCPTTTIEVLTPDFLRKDGALEQVVAAKPDVFNHNLETVPSRYLSVRPGARYFHSIRLLQRVKEIDPTIFTKSGIMVGLGEQRHEVLQVMDDLRSAEVDFLTIGQYLQPTKKHHAVMAYVTPEEFSNYETVAYTKGFLMVSASPLTRSSHHAGEDFAKLKAARDALAR

Gene
lipA
Protein
Lipoyl synthase
Organism
Bradyrhizobium sp. (strain ORS 278)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.191 kDa
Sequence
MVTIVDINANTPLRPRHPEKVNRPDSVSPAKPAWIRVKAPTTRGYADTRNIVRENGLVTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVKTGMPAALDAGEPEHVAEATFKLGLAHVVVTSVDRDDLADGGAAHIAETIRAIRAKCPTTTIEVLTPDFLRKDGALEQIVAAKPDVFNHNLETVPSRYLSVRPGARYFHSIRLLQRVKEIDPTIFTKSGIMVGLGEQRHEVLQVMDDMRSAEVDFLTIGQYLQPTKKHHAVMNYVTPEEFSNYETVAYTKGFLMVSASPLTRSSHHAGEDFAKLKAARDALAR

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodopseudomonas palustris (strain BisA53)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.87 kDa
Sequence
MVVVVDTVSDKPIRPRHPEKAARPDALSPKKPDWIRVRAPTSRGYADTRAIVKENGLHTVCEEAGCPNIGECWDRKHATFMIMGDTCTRACAFCNVKTGMPAALDGAEPANVAEATAKLGLAHLVITSVDRDDLADGGAAHIAATIRAVRERCPSTTIEVLTPDFLRKDGALEIVVAAKPDVFNHNLETVPARYLEVRPGARYFHSIRLLQRAKEIDPTLFTKSGIMLGLGEQRSEVLQVMDDLRSADVDFLTIGQYLQPTLKHHAVMSYIPPEEFSSYESLAYAKGFLMVSSSPMTRSSHHAGADFAKLQAARAALPR

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.108 kDa
Sequence
MVVLVDTVSANPVRPRHPEKAARPDALSPKKPDWIRVRAPTTRGYGETRGIVKENGLHTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVKTGMPGALDANEPAYVAEATRKLGLQHLVITSVDRDDLADGGAAHFAATIRAVREACPTTTIEILTPDFLRKDGALEVVVAAKPDVFNHNLETVPSRYLSVRPGARYFHSIRLLQRVKELDPSIFTKSGIMVGLGEERHEVLQVMDDLRSAEVDFLTIGQYLQPTRKHHAVMRYVTPDEFAGYQTTAYAKGFLMVSASPMTRSSHHAGDDFAKLKAARAARAR

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodopseudomonas palustris (strain BisB18)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.169 kDa
Sequence
MVVVVDTVSATPIRPRHPEKAARPDSLSPKKPEWIRVRAPTSRGYADTRAIVKENGLVTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVKTGMPEALDQAEPEHVAEATFKLGLKHIVITSVDRDDLADGGAAHIAATIRAVRARCPSTTIEILTPDFLRKDGALETVVAAKPDVFNHNLETVPSRYLTVRPGARYFHSIRLLQRVKEIDPTMFTKSGIMVGLGEERHEVLQVMDDLRSADVDFLTIGQYLQPSLKHHAVMRFVTPEEFAGYESVAYSKGFLMVSSSPMTRSSHHAGDNFTKLQAARAALSR

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodopseudomonas palustris (strain BisB5)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.137 kDa
Sequence
MVVLVDTVSSTPVRPRHPEKAARPDSLSPKKPDWIRVRAPTTRGYGETRSIVKENGLVTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVKTGLPGALDPNEPAYVAEATRKLGLEHLVITSVDRDDLADGGAAHFAATIRAVREHCPTTTIEILTPDFLRKDGALDVVVAAKPDVFNHNLETVPSRYLSVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERHEVLQVMDDLRSAEVDFLTIGQYLQPTRKHHAVMRYVTPDEFGGYGKTAYAKGFLMVSASPMTRSSHHAGDDFAKLRAARAALSR

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodopseudomonas palustris (strain TIE-1)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.108 kDa
Sequence
MVVLVDTVSANPVRPRHPEKAARPDALSPKKPDWIRVRAPTTRGYGETRGIVKENGLHTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVKTGMPGALDANEPAYVAEATRKLGLQHLVITSVDRDDLADGGAAHFAATIRAVREACPTTTIEILTPDFLRKDGALEVVVAAKPDVFNHNLETVPSRYLSVRPGARYFHSIRLLQRVKELDPSIFTKSGIMVGLGEERHEVLQVMDDLRSAEVDFLTIGQYLQPTRKHHAVMRYVTPDEFAGYQTTAYAKGFLMVSASPMTRSSHHAGDDFAKLKAARAARAR

Gene
lipA
Protein
Lipoyl synthase
Organism
Phenylobacterium zucineum (strain HLK1)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.207 kDa
Sequence
MAVVIDTVGARPRHPEKQANPDTPVLRKPEWLRVRAPGSANYMATREVVKSNRLVTVCEEAGCPNIGECWDKSHATFMIMGEVCTRACAFCNVATGKPLALDPDEPARVGEATAKMGLKHVVVTSVDRDDLADGGAWHFVETIRAIRAASPATTIEILTPDFARKPVAALESVIDARPDVFNHNLETVPRLYLSIRPGARYYHSLRLLERVKERDPTQFTKSGIMVGLGESKEEVMQVMDDMRSAGVDFITIGQYLQPTRKHAPIDRFVHPDEFRALEEIARAKGFLMVSASPLTRSSHHAGEDFARLQAARLAKESAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodopseudomonas palustris (strain HaA2)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.085 kDa
Sequence
MVVLVDTVSSTPVRPRHPEKAARPDALSPKKPDWIRVRAPTTRGYGETRSIVKENGLVTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVKTGMPGALDPNEPAYVAEATRKLGLEHLVITSVDRDDLADGGAAHFAATIRAVREACPTTTIEILTPDFLRKDGALEVVVAAKPDVFNHNLETVPSRYLSVRPGARYFHSIRLLQRVKELDPTLFTKSGIMVGLGEERHEVLQVMDDLRSAEVDFLTIGQYLQPTRKHHAVMRYVTPDEFGGYAKTAYAKGFLMVSASPMTRSSHHAGDDFAKLRAARAALAR

Gene
lipA
Protein
Lipoyl synthase
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.29 kDa
Sequence
MNKKKDSLFKTIKKNNIINVITTESFSKKIIKLNKPDWIKIKIPVDTFRIREIKSALRKNNLHSVCEEANCPNLPECFNRGTATFMILGSRCTRNCPFCAVSHGKPNSLNVEEPNNLAKTIFDMGIDYVVITSVVRDDLYDGGAQHFVNCIKSIRKKNKVKIEILVPDFRGRVELILKIFNSGLPDVFNHNVENVPRLYKKVRPGADYKKSLFLLESFKKKYSNIPTKSGLMLGLGEKDTEIIQVMKDLYSNGVTLLTVGQYLQPSINHIPVQRYIPLSEFKNIKKEALSIGFTNAFCGPFVRSSYHASFQANKLIKKI

Gene
lipA
Protein
Lipoyl synthase
Organism
Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.617 kDa
Sequence
MVVVLDTVSANPVRPRHPEKVNRPDALSPPKPDWIRVRAPNSRGYADTRRIVKENGLVTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVRTGMPAALEASEPEYVAEATHKLGLAHVVVTSVDRDDLDDGGAEHFAQTIRAIRERCPATTIEILTPDFLRKDGALEKVVAAKPDVFNHNLETVPSRYLTVRPGARYFHSIRLLQRVKEIDPTIFTKSGIMVGLGEERHEVLQVMDDLRSADVDFLTIGQYLQPTRKHHAVMRYVTPDEFQGYETVGYTKGFLMVSASPLTRSSHHAGEDFAKLQTARAKLLR

Gene
lipA
Protein
Lipoyl synthase
Organism
Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255)
Length
319 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.509 kDa
Sequence
MVVILDTISANPVRPRHPEKANRPDALSPPKPDWIRVRAPNTRGYANTRRIVKENGLVTVCEEAGCPNIGECWDKKHATFMIMGDTCTRACAFCNVKTGMPGAIESSEPEYVAEATRKLGLAHVVVTSVDRDDLDDGGAEHFAQTIRAIRERCPATTIEILTPDFLRKDGALEKVVAAKPDVFNHNLETVPSRYLTVRPGARYFHSIRLLQRVKEIDPAIFTKSGIMVGLGEERHEVLQVMDDLRSADVDFLTIGQYLQPTRKHHAVIRYVTPEEFSSYETVAYTKGFLMVSASPLTRSSHHAGEDFAKLQAARATLSR

Gene
lipA
Protein
Lipoyl synthase
Organism
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Length
318 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.73 kDa
Sequence
MARPKVEAGVKLRGAEKVARIPVKIIPTVDLPKKPDWIRVRIPVSPEVDRIKQLLRKHKLHSVCEEASCPNLGECFSGGTATFMIMGDICTRRCPFCDVGHGRPKALDADEPKSLAIAIADLRLKYVVITSVDRDDLRDGGAQHFADCIREIRLLSPGIQLETLVPDYRGRMDVALEITAAEPPDVFNHNLETVPRLYKAARPGSDYQWSLTLLQRFKQMVPHVPTKSGLMLGLGETDEEVIEVMKRMREHDIDMLTLGQYLQPSRNHLAVQRFVHPDTFAWFAEEGYKMGFKNVASGPLVRSSYHADEQAKIAKAML

Gene
lipA
Protein
Lipoyl synthase
Organism
Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.617 kDa
Sequence
MVTVVDKVTSMRVRHPEKAHRPDTSIQKKPDWIRVKAPTSQVYKETHGIVRANKLVTVCEEAGCPNVGECWSQRHASFMILGEICTRACAFCNVATGIPLAVDDDEPERVADAVAQMGLKHVVITSVDRDDLADGGAQHFAKVIYAIRRKSLGTTIEVLTPDFRHKDHALEIVVAAKPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKEIDPMIFTKSGIMVGFGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFLPPDEFESFAKIGKAKGFLHMASSPLTRSSHHAGDDFEILKKARAQKFS

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium gilvum (strain PYR-GCK)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.584 kDa
Sequence
MSIAPDGRKLLRLEVRNAETPIERKPPWIKTRAKMGPEYKELKALVRREGLHTVCEEAGCPNIFECWEDREATFLIGGEQCTRRCDFCQIDTGKPADLDRDEPRRVAESVQAMGLRYSTVTGVARDDLPDGGAWLYAETVRQIKALNPNTGVELLIPDFNADPDQLRAVFESRPEVLAHNVETVPRIFKRIRPGFRYERSLAVITAARDYGLVTKSNLILGMGETPEEVRAALHDLHDAGCDIVTITQYLRPSPRHHPVERWVHPDEFVDHERYATEIGFAGVLAGPLVRSSYRAGKLYAQTVAKRSAVSLSNGEIA

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.148 kDa
Sequence
MDSQPQSKKAARGADKTARNPIPIIPAPTERLPKPQWLRVRSPLSPEVDQLKKILRDAALHTVCEEASCPNLGECFGGGTATFMILGDICTRRCPFCDVAHGRPEAPDPLESVHLARTVASMKLRFVVITSVDRDDLRDGGARHFAEVISALREHCPELHVEILVPDFRGRVANALAAFRETPPDVFNHNLETVPRLYLQARPGADYHHSLQLLAAFKAQHPQIPTKSGLMLGLGEEIDEIRGVMRDLRQAGCELLTIGQYLAPSRHHLPVARFVPPEEFQQLQRDGMAMGFRHVASGPLVRSSYHAERSFHEIGGD

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.148 kDa
Sequence
MDSQPQSKKAARGADKTARNPIPIIPAPTERLPKPQWLRVRSPLSPEVDQLKKILRDAALHTVCEEASCPNLGECFGGGTATFMILGDICTRRCPFCDVAHGRPEAPDPLESVHLARTVASMKLRFVVITSVDRDDLRDGGARHFAEVISALREHCPELHVEILVPDFRGRVANALAAFRETPPDVFNHNLETVPRLYLQARPGADYHHSLQLLAAFKAQHPQIPTKSGLMLGLGEEIDEIRGVMRDLRQAGCELLTIGQYLAPSRHHLPVARFVPPEEFQQLQRDGMAMGFRHVASGPLVRSSYHAERSFHEIGGD

Gene
lipA
Protein
Lipoyl synthase
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.085 kDa
Sequence
MSAVAPDGRKMLRLEVRNSQTPIERKPEWIKTRAKMGPEYTKMQNLVKSEGLHTVCQEAGCPNIYECWEDREATFLIGGDQCTRRCDFCQIDTGKPEALDRDEPRRVGESVVTMDLNYATITGVARDDLPDGGAWLYAETVRQIHEQTAGREAGRTKVELLAPDFNAVPELLREVFESRPEVFAHNVETVPRIFKRIRPGFRYERSLKVITDARDFGLVTKSNLILGMGETREEISEALKQLHEAGCELITITQYLRPSVRHHPVERWVKPQEFVELKEEAEQIGFSGVMSGPLVRSSYRAGRLYGMAMEQRRSATV

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.148 kDa
Sequence
MDSQPQSKKAARGADKTARNPIPIIPAPTERLPKPQWLRVRSPLSPEVDQLKKILRDAALHTVCEEASCPNLGECFGGGTATFMILGDICTRRCPFCDVAHGRPEAPDPLESVHLARTVASMKLRFVVITSVDRDDLRDGGARHFAEVISALREHCPELHVEILVPDFRGRVANALAAFRETPPDVFNHNLETVPRLYLQARPGADYHHSLQLLAAFKAQHPQIPTKSGLMLGLGEEIDEIRGVMRDLRQAGCELLTIGQYLAPSRHHLPVARFVPPEEFQQLQRDGMAMGFRHVASGPLVRSSYHAERSFHEIGGD

Gene
lipA
Protein
Lipoyl synthase
Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.148 kDa
Sequence
MDSQPQSKKAARGADKTARNPIPIIPAPTERLPKPQWLRVRSPLSPEVDQLKKILRDAALHTVCEEASCPNLGECFGGGTATFMILGDICTRRCPFCDVAHGRPEAPDPLESVHLARTVASMKLRFVVITSVDRDDLRDGGARHFAEVISALREHCPELHVEILVPDFRGRVANALAAFRETPPDVFNHNLETVPRLYLQARPGADYHHSLQLLAAFKAQHPQIPTKSGLMLGLGEEIDEIRGVMRDLRQAGCELLTIGQYLAPSRHHLPVARFVPPEEFQQLQRDGMAMGFRHVASGPLVRSSYHAERSFHEIGGD

Gene
lipA
Protein
Lipoyl synthase
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.085 kDa
Sequence
MSAVAPDGRKMLRLEVRNSQTPIERKPEWIKTRAKMGPEYTKMQNLVKSEGLHTVCQEAGCPNIYECWEDREATFLIGGDQCTRRCDFCQIDTGKPEALDRDEPRRVGESVVTMDLNYATITGVARDDLPDGGAWLYAETVRQIHEQTAGREAGRTKVELLAPDFNAVPELLREVFESRPEVFAHNVETVPRIFKRIRPGFRYERSLKVITDARDFGLVTKSNLILGMGETREEISEALKQLHEAGCELITITQYLRPSVRHHPVERWVKPQEFVELKEEAEQIGFSGVMSGPLVRSSYRAGRLYGMAMEQRRSATV

Gene
lipA
Protein
Lipoyl synthase
Organism
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.982 kDa
Sequence
MVTVIDTLARPRHPEKANRPETEVLRKPDWIRVKAPGSAGWSQTAEIVRANGLHTVCEEAGCPNIGECWEKKHATFMIMGDTCTRACAFCNVRTGMPEALDQGEPQKVGDAVAKLGLSHVVITSVDRDDLADGGAEHFARTIAAIRKASPGTTIEILTPDFLRKDGALEVVVAARPDVFNHNLETVPAKYLSVRPGARYFHSLRLLQKVKELDGSIFTKSGIMVGLGEERPEVLQLMDDLRSAEVDFITIGQYLQPTRKHHKVERFVTPDEFKAYETVAYAKGFLMVSASPLTRSSHHAGDDFEKLRAARVARLGRS

Gene
lipA
Protein
Lipoyl synthase
Organism
Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)
Length
317 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.168 kDa
Sequence
MVTVVNTLNRPRHPEKQNRPETEVLRKPDWIRVKAPGSAGWSNTAGIVRANGLHTVCEEAGCPNIGECWEKKHATFMIMGDTCTRACSFCNVRTGMPKALDLDEPQKVGEAVAKLGLSHVVITSVDRDDLTDGGAEHFARTIASIRKLSPGTTIEILTPDFLRKPGAIEVVVAARPDVFNHNLETVPGKYLTVRPGARYFHSLRLLQQVKELDPSIFTKSGIMVGLGEERNEVLQLMDDLRAAEVDFMTIGQYLQPTRKHHKVERFVTPDEFKAYETVAYAKGFLMVSSSPLTRSSHHAGDDFAKLRAAREAKLGRI

Gene
lipA
Protein
Lipoyl synthase
Organism
Hydrogenovibrio crunogenus (strain XCL-2)
Length
316 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.7 kDa
Sequence
MKARNESMSKGEYKTKSLKNRPDPTQPKLKKPSWIKAKLPSAKHIGRVKELKQVLREQGLNSVCEEASCPNLGECFGHGTATFMIMGHICTRKCPFCDVTHGRPNPLNQDEPRHLAKTIHAMNLNYVVITSVDRDDLRDGGATHFKNCTQAIRDKMPDIQIETLVPDFRGRLTVALDILAQQAPDVLNHNLETVPRLYEEARPGADYQASLDLLKRFKQMVPETKTKSGLMVGLGETFDEILQVMRDLRAHDVEMLTVGQYLQPSDFHLAVQRYWTPEEFKQLEQAGMEMGFTHVASGPMVRSSYHADLQAQGQFS

Gene
lipA
Protein
Lipoyl synthase
Organism
Wigglesworthia glossinidia brevipalpis
Length
316 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.2 kDa
Sequence
MKSISYLNTKEKNKKKLSIPSKTIFAKENEYGLKKPNWLKIKLPLNNKKINKIKLIMRKNNLHTVCEEAACPNLAECFNRGTATFMILGSICTRRCPFCNVSSGRPSLVDTKEPENLSKAAIKMKLKHIVITSVDRDDLKDGGSEHFSNCIRFIRKKNPDIKIEILVPDFRGCTELALNNISTYPPDIFNHNLESIPRLYSKVRPGANYKRSLELLEKFNLINPNIPTKSGLMLGLGETKEEIIEVMKDLRKSYVSMITIGQYLRPTKNHLTVNRYVHPKEFRELNLIAFDLGFKHAMCGPLVRSSYHAENQINCY

Gene
lipA
Protein
Lipoyl synthase
Organism
Ruegeria sp. (strain TM1040)
Length
316 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.106 kDa
Sequence
MRDLKIPEQRHPEKAHRPDNAQPKKPSWIRVKAPGGKGYAETHKIMRENNLVTVCEEAGCPNVGECWSQGHATMMIMGEICTRGCTFCNIATGRPDTLDAFEPGRVAHAVQKLGLNHVVITSVDRDDLEDGGADHFAQTIRAVRHRSPQTTIEILTPDFLKCAPEVLETVVEAKPDVFNHNLETVPGLYPEVRPGARYFHSLRLLQRVKELDPSIFTKSGIMVGLGEQAPQVKQVMDDMRAADVDFLTIGQYLQPTPKHHAVDRFVTPEEFESYEKAAYGKGFLMVSATPLTRSSYHAGDDFAKLRAARNAKLGLA

Gene
lipA
Protein
Lipoyl synthase
Organism
Nocardioides sp. (strain ATCC BAA-499 / JS614)
Length
316 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.917 kDa
Sequence
MTQAPPSPQAEGRKLLRLEARNSETPIERKPEWIKTRAKMGPEYQHLQNLVKSEGLHTVCQEAGCPNIYECWEDREATFLIGGEQCTRRCDFCQIDTGRPKPLDRDEPRRVAESVRTMGLRYATITGVTRDDLIDEGAWLYAETVRQIHELNPGIGVENLIPDFSGKPDLLAQVFESRPEVLAHNLETVPRIFKRIRPAFRYDRSLDVLTQARDFGLVTKSNLILGLGETREEVSQALRDLHAAGCELLTITQYLRPSPRHHPVERWVKPEEFVELKDEADEVGFTGVMSGPLVRSSYRAGRLYRQAVEAREGVTA

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Length
316 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.25 kDa
Sequence
MIFCLSSGQTPMAFRLPVVAEPEMPAGTDVSSTGRLPRWLKRPIPKSNSNHLTDSLMEEYGLETVCDNAKCPNRMECYSQQTATFMVLGNVCTRPCGFCAVSRGRPPAAPAVDEPDRIAKAAERLGLKHVVITSVTRDDLPDGGADHFHNCVIAVRERTGATTEVLTPDFVHCKEALARVIEAKPTVFNHNMETVPRLYRRVRGPKSDYAWTLEMMRQVKRYDAEVKTKSGLMLGLGEERGELLDALSDLREHDVDFLTLGQYLQPGEKYLPVVRYVPPEEFDELADIAKSMGFKKVASGPFVRSSYHARDMAETE

Gene
lipA
Protein
Lipoyl synthase
Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71)
Length
316 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.69 kDa
Sequence
MTIESRQKGVAKTARNPVKIAPQSTDQLLRKPSWIRVRSSNSQEFYEVKRILREQKLHTVCEEASCPNIGECFGKGTATFMILGDLCTRRCPFCDVAHGRPRPPDPEEPLHLAQSIAAMKLKYVVITSVDRDDLRDGGAQHFVDCIREVRAHSPQTKIEILVPDFRGRLDIALEKLFACPPDVMNHNLETVPRLYRQCRPGADYTHSLRLLKEFKARFPGIPTKSGLMLGLGETDEEILDVMRDLRKHDVEMLTIGQYLQPSIGHLPVMRYVTPGAFKEFERAAIEMGFSNAACGPMVRSSYHADQQAHEAGIIQR

Gene
lipA
Protein
Lipoyl synthase
Organism
Laribacter hongkongensis (strain HLHK9)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.334 kDa
Sequence
MKQDNQTGIKHKGEAKTARIPIKVVPLEEKLRKPEWIRAKLPTGQRFFEIKEILRNQKLHTVCEEASCPNIGECFSHGTATFMIMGDICTRRCPFCDVGHGRPNPLDPNEPQHLAESVAAMRLKYVVITSVDRDDLRDGGAQHFADCIQAIRASSPATRIEVLVPDFRGRLELALDILSATPPDVMNHNLETAPRLYKQARPGADYAHSLQLLKDYKTRNPDVTTKSGIMVGLGETDEEVLEVLADLRAHDVDMLTIGQYLQPSNGHLPVLRYVTPDQFKAFEKKAYDMGFRHAAVGAMVRSSYHADQQAREVIE

Gene
lipA
Protein
Lipoyl synthase
Organism
Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.159 kDa
Sequence
MFQEIDIKSLKGKSKVARLRIKPDVNRTVIRKPKWIRTKHIFGSKVDQLKSTLRAQKLFTVCEEAQCPNLVECFNHGTATFMIMGQICTRRCPFCDVAHGKPRTLDIDEPKHLADTIKKMRLKYVVITSVDRDDLHDGGVQHFKMCIDNIRLSTPKVKIEILTPDFKGRIDKALKVFKSCPPDVFNHNLETVPSLYPKVRPGANYEYSLKLLQKFKQQHPLVISKSGLMLGVGESEKQVINVLKDLRRHNVDMLTIGQYLQPSKYHLAVETYIHPNQFDKYRKIALKLGFIRVASGPMVRSSYHANLQIKGKLII

Gene
lipA
Protein
Lipoyl synthase
Organism
Coxiella burnetii (strain CbuK_Q154)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.574 kDa
Sequence
MTTYDPSQKSLGKEKLSRIPVKIEATHTPLRKPDWIRIRLSTDSKVSQLKKLLRENHLVTVCEEASCPNLNECFGHGTATFMIMGDKCTRRCSFCDVGHGRPDPLDPEEPVNLANTVSIMSLRYVVITSVDRDDLRDGGAQHYAQCINAVREKNPGIKVEVLVPDFRGRMEKALDQLAQGLPDVFNHNIETAPRLYKQARPGADYPWSLALLQTFKKRFPGIPTKSGMMLGLGETREEVETVMRDLRQHEVDRLTLGQYLQPTRYHMPVDRYVTPQEFQELGELAKKLGFSNVASGPLVRSSYHADLQAQGERVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Coxiella burnetii (strain CbuG_Q212)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.604 kDa
Sequence
MTTYDPSQKSLGKEKLSRIPVKIEATHTPLRKPDWIRIRLSTDSKVSQLKKLLRENHLVTVCEEASCPNLNECFGHGTATFMIMGDKCTRRCSFCDVGHGRPDPLDPEEPVNLANTVSIMSLRYVVITSVDRDDLRDGGAQHYAQCINAVREKNPGIKVEVLVPDFRGRMEKALDQLAQGLPDVFNHNIETAPRLYKQARPGADYPWSLALLQTFKKRFPGIPTKSGMMLGLGETREEVEMVMRDLRQHEVDRLTLGQYLQPTRYHMPVDRYVTPQEFQELGELAKKLGFSNVASGPLVRSSYHADLQAQGERVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Coxiella burnetii (strain Dugway 5J108-111)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.574 kDa
Sequence
MTTYDPSQKSLGKEKLSRIPVKIEATHTPLRKPDWIRIRLSTDSKVSQLKKLLRENHLVTVCEEASCPNLNECFGHGTATFMIMGDKCTRRCSFCDVGHGRPDPLDPEEPVNLANTVSIMSLRYVVITSVDRDDLRDGGAQHYAQCINAVREKNPGIKVEVLVPDFRGRMEKALDQLAQGLPDVFNHNIETAPRLYKQARPGADYPWSLALLQTFKKRFPGIPTKSGMMLGLGETREEVETVMRDLRQHEVDRLTLGQYLQPTRYHMPVDRYVTPQEFQELGELAKKLGFSNVASGPLVRSSYHADLQAQGERVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Coxiella burnetii (strain RSA 331 / Henzerling II)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.604 kDa
Sequence
MTTYDPSQKSLGKEKLSRIPVKIEATHTPLRKPDWIRIRLSTDSKVSQLKKLLRENHLVTVCEEASCPNLNECFGHGTATFMIMGDKCTRRCSFCDVGHGRPDPLDPEEPVNLANTVSIMSLRYVVITSVDRDDLRDGGAQHYAQCINAVREKNPGIKVEVLVPDFRGRMEKALDQLAQGLPDVFNHNIETAPRLYKQARPGADYPWSLALLQTFKKRFPGIPTKSGMMLGLGETREEVEMVMRDLRQHEVDRLTLGQYLQPTRYHMPVDRYVTPQEFQELGELAKKLGFSNVASGPLVRSSYHADLQAQGERVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.604 kDa
Sequence
MTTYDPSQKSLGKEKLSRIPVKIEATHTPLRKPDWIRIRLSTDSKVSQLKKLLRENHLVTVCEEASCPNLNECFGHGTATFMIMGDKCTRRCSFCDVGHGRPDPLDPEEPVNLANTVSIMSLRYVVITSVDRDDLRDGGAQHYAQCINAVREKNPGIKVEVLVPDFRGRMEKALDQLAQGLPDVFNHNIETAPRLYKQARPGADYPWSLALLQTFKKRFPGIPTKSGMMLGLGETREEVEMVMRDLRQHEVDRLTLGQYLQPTRYHMPVDRYVTPQEFQELGELAKKLGFSNVASGPLVRSSYHADLQAQGERVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.337 kDa
Sequence
MKPDNQAGVKHKGAAKTARIPIKIVPLDEKLKKPEWIRAKLPNGQRFHEIKQILREQKLHTVCEEATCPNIGECFSKGTATFMIMGDICTRRCPFCDVGHGRPNPLDENEPRHLAESVAAMRLKYVVVTSVDRDDLRDGGAQHFADCINAVREMSPATQIETLVPDFRGRLDIAVDILTQTPPDVMNHNLETVPRLYKQARPGADYAHSLQLLKDYKAKNPNVRTKSGLMVGLGETDEEILEVMRDLRAHNVDMLTIGQYLQPSDGHLPVLRYVHPDVFKMFEEKAYEMGFVHAAVGAMVRSSYHADVQAHEAGV

Gene
lipA
Protein
Lipoyl synthase
Organism
Ruthia magnifica subsp. Calyptogena magnifica
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.868 kDa
Sequence
MLQEIDIKSLKGKSKVVRLKIKPDSERLPIKKPNWIRIKHVASQKVEQLKKTLRSQKLFTVCEEAQCPNLSECFNHGAATFMIMGQICTRRCPFCDVAHGKPKALDVDEPKHLANTIKKMQLKYVVITSVDRDDLRDGGAQHFKTCIDNIRLSTPKVKIEILTPDFRGRIDKVLEVFKSCSPNVFNHNLETVPSLYQKVRPGANYNYSLRLLKAFKQQHPFVITKSGLMLGVGESEKQVINVLKDLRKHNVDMLTLGQYLQPSKHHLAVEAYIHPNQFDKYKKIALKLGFSQVASGPMVRSSYHADLQIKGELIS

Gene
lipA
Protein
Lipoyl synthase
Organism
Aromatoleum aromaticum (strain EbN1)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.292 kDa
Sequence
MDSTARKQRGADKTARIPIKIVPAERLKKPEWIRIRLGAGHEAERFNEIKASLREHKLHTVCEEASCPNIHECFGKGTATFMIMGDICTRRCPFCDVGHGRPEPLNANEPQELAATIGAMRLNYVVITSVDRDDLRDGGAQHFVDCIRETRAASPKTRIEVLVPDFRGRLDVALEIFDQAPPDVMNHNLETVPRLYKQARPGADYAYSLRLLKEFKARHPDVPTKSGLMVGLGETDDEILDVLRDLRAHDVEMLTIGQYLQPSTGHLPVLRYVHPDTFKMFETEALAMGFKNAACGPMVRSSYWADQQAYGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Azoarcus sp. (strain BH72)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.336 kDa
Sequence
MDNPARKQRGAEKTARIPIKIVPAERLKKPDWIRIRLGAGAEAERFNEIKQTLREHKLHTVCEEASCPNIHECFGKGTATFMIMGDICTRRCPFCDVGHGRPEPLNPNEPTDLARTIAAMRLNYVVITSVDRDDLRDGGAQHFVDCIRETRAASPSTTIEVLVPDFRGRMEIALEIFNQAPPDVMNHNMETVPRLYKQARPGADYAYSLRLLKEFKAGHPDVLTKSGLMVGLGETDDEILDVMRDLRAHDVDMLTIGQYLQPSGGHLPVLRYVHPDTFKMFETEALRMGFRNAACGPMVRSSYWADQQAHGAGVV

Gene
lipA
Protein
Lipoyl synthase
Organism
Paracoccus denitrificans (strain Pd 1222)
Length
315 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.98 kDa
Sequence
MADMPPVLRHPEKAHRPDQPQPKKPDWIRVKAPTSQGYKDTRDILRNNRLSTVCEEAGCPNVGECWSQGHATMMIMGEICTRGCSFCNVMTGKPNALDVFEPGRVAHAVQKLGLKHVVITSVDRDDLDDGGAEHFAQTIRAIRHRSPASTIEVLTPDFLKSKPGALEAVVEARPDVFNHNLETVPGLYPTVRPGARYFHSLRLLQQVKELDPGMFTKSGIMVGLGEDRQGILQVMDDMRAADVDFITIGQYLQPTPKHHRVDRFVTPEEFKGYEKAAYGKGFLMVSATPLTRSSYHAGDDFAQLRAARLAKLGRA

Gene
lipA
Protein
Lipoyl synthase
Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.103 kDa
Sequence
MMDTPIIRHPEKVRRPDNPSPRKPEWIRVRAPVSHEAAEVRQLMRSKNLFTVCEEAACPNIGECWKRRHATFMILGDICTRACAFCNVRTGKPGHVDDQEPVNLADSVVAMGLKHVVITSVDRDDLADGGAGHFHRCITEVRSRAPSCSIEVLTPDFRDKPQGALARVVEAGPDVFNHNLETVPRLYPTIRPGARYFHSLKLLDRVKTIDPGVFTKSGIMVGLGETREEVLQVMDDMRSAGVDFLTIGQYLQPTLKHVAVDRFVTPDEFKDYADIARGKGFLMVASSPLTRSSHHADRDFEDLRKARQDAAATK

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium leprae (strain Br4923)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.12 kDa
Sequence
MTVAPEDCRLLRLEVRNAQTPIERKPPWIKTRARMGPEYTALKNLVRRVALHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAALDRDEPRRVAESVQTMGLRYTTVTGVARDDLPDGGAWLYATTVRAIKELNPSTGVELLIPDFNGQPARLAEVFDSRPQVLAHNVETVPRIFKRIRPAFTYQRSLDVLTAAREAGLVTKSNLILGLGETADEVRTALADLRKTGCDIVTITQYLRPSMRHHPVERWVRPEEFVEYTQYAEGLGFSGVLGGPLVRSSYRAGRLYEQAAGTRTVGTSVSR

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium leprae (strain TN)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.12 kDa
Sequence
MTVAPEDCRLLRLEVRNAQTPIERKPPWIKTRARMGPEYTALKNLVRRVALHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAALDRDEPRRVAESVQTMGLRYTTVTGVARDDLPDGGAWLYATTVRAIKELNPSTGVELLIPDFNGQPARLAEVFDSRPQVLAHNVETVPRIFKRIRPAFTYQRSLDVLTAAREAGLVTKSNLILGLGETADEVRTALADLRKTGCDIVTITQYLRPSMRHHPVERWVRPEEFVEYTQYAEGLGFSGVLGGPLVRSSYRAGRLYEQAAGTRTVGTSVSR

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.412 kDa
Sequence
MTVVPEGRKLLRLEVRNAQTPIERKPPWIKTRAKMGPEYTELKGLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGEQCTRRCDFCQIDTGKPADLDRDEPRRVAESVQAMGLRYSTVTGVARDDLPDGGAWLYAETVRYIKRLNPNTGVELLIPDFNGNPEQLEEVFESRPEVLAHNVETVPRIFKRIRPAFRYDRSLAVITAARNFGLVTKSNLILGMGETIDEVRTALRDLHDAGCDIITITQYLRPSPRHHPVERWVHPDEFVELSAYAEGLGFAGVLAGPLVRSSYRAGKLYAQAARVRFADQPPVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.484 kDa
Sequence
MDVQPTTMRGAVKTAHLGTDVSLATKPLPKPEWLRGKSASTPDVERLVRILRDNRLHTVCEEASCPNLGECFRKGTATFMIMGDVCTRHCPFCNVAHGSPHELAADEPVNLARAVELLKLSYVVITSVTRDDLPDGGAGHYGACVRALRDLKRSLKVEILTPDFRGAVAVAFEELRMNLPDVFNHNLETVPRLYPRVRPQADYHGSLDLLLRFREQFDHVPTKSGLMLGLGETEQEVRDVMEELRRHRCDMLTLGQYMRPSPHHLPVERYVTPDEFERYRQFGLSIGFSHVESGPMVRSSYHADMQARELMLVN

Gene
lipA
Protein
Lipoyl synthase
Organism
Dechloromonas aromatica (strain RCB)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.628 kDa
Sequence
MAEKGVKQKGELKTARIPIKIVPVDTPLRKPEWIRVKAGNSAGRFGEIKSMLREKKLHTVCEEAACPNIGECFGRGTATFMILGDICTRRCPFCDVGHGQPLPPNPNEPAELADSVSSLKLQYVVITSVDRDDLRDGGAQHFVDVVRAVREASPKTTIETLVPDFRGRMDIAIDILGNGLPDVLNHNMETVPRLYKQARPGADYAHSLALMKQFKARYPDVKTKSGLMVGLGETDEEILEVMRDLRANDVEMLTIGQYLAPSGHHLPVSRYVHPDTFKMFEEEAKKMGFSGAACAPMVRSSYWADQQAHSAGVA

Gene
lipA
Protein
Lipoyl synthase
Organism
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.892 kDa
Sequence
MSNQQTHVRKPDWLKTRINTNKSYRNLKKLMRDNRLNTVCEEARCPNLHECWSERKTATFMILGDTCTRGCRFCAVKTGLPNELDWGEPERVADSVTVMGLKHVVVTAVARDDLNDGGAAVFAETVRAIRRKNPGCTIEILPSDMKGDYESLHTLMDSGPDIFNHNIETVRRLTKRVRARAMYDRSLELLRRVKEIAPNTPTKSSIMVGLGEEKDEIIQAMDDLLAHNVDIVTLGQYLQPTKKHLEVVRYYHPDEFEELKNIALEKGFSHCESGPLVRSSYHADEQVSNAAAQRRIKYMKGVEKQENSQLDFNF

Gene
lipA
Protein
Lipoyl synthase
Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
36.202 kDa
Sequence
MRTKNSKIINSEQDIFRNKVIPIKFLSNYNNEILKKPQWMKIKFPVSTNKIKNLTLILRQHNLNTVCEQALCPNLAECFNRGTATFMILGSICTRRCPFCAVSHGKPSLVNKNEPQQLARVIFDMKINYVVITSVVRDDLKDRGAQHFSNCIQEIRNKNNVKIEILVPDFRGMMRESCKIISMNPPNVFNHNLENVPRLYKLIRPGASYIRSLKLLEFFKKLNPNVPTKSGLILGLGETYKEIVHVINDLLDHGVTILTIGQYLQPSSKHFPVQKYITPDEFKKIKNYALSIGFKKVFCGPLIRSSYHAEKYFE

Gene
lipA
Protein
Lipoyl synthase
Organism
Nitrosomonas eutropha (strain DSM 101675 / C91)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.156 kDa
Sequence
MVADTHQRGTAKTARNPIKIDLEQSGQLLRKPSWIRVRSPNSQRYQEVKRLLRENKLHTVCEEASCPNIGECFGRGTATFMILGDLCTRRCPFCDVAHGRPHAPDPDEPMHLAKSIAVLKLNYVVITSVDRDDLRDGGAQHFADCIRAIRAQSPQTRIEILVPDFRGRLEIALEKLSACPPDVMNHNLETVPRLYKQCRPGADYVHSLQLLKDFKAASPHIPTKSGLMLGLGETDEEIIGVMQDLRAHQVNMLTIGQYLQPSIGHHPVMRYVSPEDFKTFERIATNLGFSHAACGPMVRSSYHADQQAHEAGIE

Gene
lipA
Protein
Lipoyl synthase
Organism
Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
Length
314 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.255 kDa
Sequence
MAADTHQRGAAKTARNPVKIDLEQSGQLLRKPSWIRVRSSNSQKYLEVKRLLRENRLHTVCEEASCPNIGECFGRGTATFMILGDLCTRRCPFCDVAHGRPHAPDPDEPMHLANSIAVLKLNYVVITSVDRDDLRDGGAQHFADCIRAIRTQSPQTRIEILVPDFRGRLEVALEKLSACPPDVMNHNLETVPRLYKQCRPGADYMHSLQLLKDFKAAFPHIPTKSGLMLGLGETDEEIIEVMRDLRAHQVDMLTVGQYLQPSKGHHPVMRYVSPEDFKTFERIATNLGFSHAACGPMVRSSYHADQQAHEAGIE

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)
Length
313 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.845 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLHTVCEEAKCPNIHECWGERRTATFMILGAVCTRACRFCAVKTGLPNELDLDEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTSIEILPSDMGGDYDALETLMASKPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSLMVGLGETHEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVEKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKERHRIGEEKLGNEIGTDTNN

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)
Length
313 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.845 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLHTVCEEAKCPNIHECWGERRTATFMILGAVCTRACRFCAVKTGLPNELDLDEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTSIEILPSDMGGDYDALETLMASKPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSLMVGLGETHEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVEKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKERHRIGEEKLGNEIGTDTNN

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlamydophila caviae (strain GPIC)
Length
312 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.969 kDa
Sequence
MNTPSDETRKPPQGKRFAERLPKWLRQVLPTGPVFAQTDTTIKRTGMATVCEEALCPNRACCWSRKTATYLALGDACTRRCGFCNIDFTKKPISPDPEEPQKIAESAKILQLKHIVLTMVARDDLEDGGASFLVRIIDTLHQELPESTVEVLASDFQGNIDALHTLLDSGLTIYNHNVETVERLTPVVRHKATYRRSLFMLEQAAMYLPDLKIKSGIMVGLGEQESEVKQTLKDLADHGVKIVTIGQYLRPSRSHIPVKSYVTPETFDYYRTIGTSLGLFVYAGPFVRSSFNADIVLHNLENKQSDVAKMQN

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlamydia felis (strain Fe/C-56)
Length
312 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.12 kDa
Sequence
MNEAPAEKQKPQQGKRFSERLPQWLRQVLPRGSVFTHTDATLKRTGLATVCEEALCPNRTHCWSRKTATYLALGDTCSRRCGFCNIDFSKNPLPPDPEEPQKIAESAKALQLKHIVLTMVARDDLEDGGASYLARIIHTLHQELPESTIEVLASDFQGNVDALHVLLDSGLTIYNHNVETVERLTPVVRHKATYRRSLFMLEQAAVYLPNLKIKSGIMVGLGEQESEVKQTLKDLADHGVRIVTIGQYLRPSRLHIPVKNYVTPETFDYYRSVGESLGLFVYAGPFVRSSFNADMVLHNLQDKQSEIAKVPR

Gene
lipA
Protein
Lipoyl synthase
Organism
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Length
312 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.408 kDa
Sequence
MSEPLPITDAPKQRKPDWIRVKAPMGQAFSDTKALMRRLNLATVCEEAACPNIGECWTKKHATVMILGDTCTRACAFCNVKTGMPRPVDALEPQHVADAAAELGLEHIVVTSVDRDDLPDGGAKQFVKVIEALRRTTPRTTIEILTPDFRNKADAAIEMIVAARPDVYNHNLETVPRLYPTIRPGARYYASLRLLETVKRLDPTIFTKSGIMVGLGEERLEVHQVMDDMRSADIDFLTMGQYLQPTPKHAKVADFVAPKTFEAYAAIARAKGFLLVAATPLTRSSYHAGDDFVKLRDARNAELARKAAVPAA

Gene
lipA
Protein
Lipoyl synthase
Organism
Thermobifida fusca (strain YX)
Length
312 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.223 kDa
Sequence
MSIAPEGRRLLRIEARNSTTPIEKKPPWIKIRAKMGSEYTELHALVKREGLHTVCQEAGCPNIYECWEDREATFLIGGDQCTRRCDFCQIATGKPAALDRGEPLRVAESVRTMGLKYATVTGVARDDLDDGGAWLYAETVRKIHELNPGTGVELLIPDFNADPDLLAEVFSSRPEVLAHNIETVPRIFKRIRPGFRYERSLEVITRAREAGLVTKSNLILGMGETREEISQAMRDLYEAGCDLLTITQYLRPSRLHHPVDRWVKPEEFVELGREAEEIGFAGVMSGPLVRSSYRAGRLYRQAIERRKADAKS

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)
Length
312 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.157 kDa
Sequence
MQRGRRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSGRDGPGTATFMLMGDRCSRGCNFCDVETGGMKSLDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGPDVIAHNVETVERLQWPVRDRRADYEQSLAVLDRVGRESDIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQPSRSHLDVFEYVHPDVFETWRAVAEREFDFLYCASGPMVRSSYKAGELFVEALLREGRSPEDARRHARAAGGD

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.719 kDa
Sequence
MSVAAEGRRLLRLEVRNAQTPIERKPPWIKTRARIGPEYTELKNLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDRDEPRRVADSVRTMGLRYATVTGVARDDLPDGGAWLYAATVRAIKELNPSTGVELLIPDFNGEPTRLAEVFESGPEVLAHNVETVPRIFKRIRPAFTYRRSLGVLTAARDAGLVTKSNLILGLGETSDEVRTALGDLRDAGCDIVTITQYLRPSARHHPVERWVKPEEFVQFARFAEGLGFAGVLAGPLVRSSYRAGRLYEQARNSRALASR

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.719 kDa
Sequence
MSVAAEGRRLLRLEVRNAQTPIERKPPWIKTRARIGPEYTELKNLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDRDEPRRVADSVRTMGLRYATVTGVARDDLPDGGAWLYAATVRAIKELNPSTGVELLIPDFNGEPTRLAEVFESGPEVLAHNVETVPRIFKRIRPAFTYRRSLGVLTAARDAGLVTKSNLILGLGETSDEVRTALGDLRDAGCDIVTITQYLRPSARHHPVERWVKPEEFVQFARFAEGLGFAGVLAGPLVRSSYRAGRLYEQARNSRALASR

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.719 kDa
Sequence
MSVAAEGRRLLRLEVRNAQTPIERKPPWIKTRARIGPEYTELKNLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDRDEPRRVADSVRTMGLRYATVTGVARDDLPDGGAWLYAATVRAIKELNPSTGVELLIPDFNGEPTRLAEVFESGPEVLAHNVETVPRIFKRIRPAFTYRRSLGVLTAARDAGLVTKSNLILGLGETSDEVRTALGDLRDAGCDIVTITQYLRPSARHHPVERWVKPEEFVQFARFAEGLGFAGVLAGPLVRSSYRAGRLYEQARNSRALASR

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.719 kDa
Sequence
MSVAAEGRRLLRLEVRNAQTPIERKPPWIKTRARIGPEYTELKNLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDRDEPRRVADSVRTMGLRYATVTGVARDDLPDGGAWLYAATVRAIKELNPSTGVELLIPDFNGEPTRLAEVFESGPEVLAHNVETVPRIFKRIRPAFTYRRSLGVLTAARDAGLVTKSNLILGLGETSDEVRTALGDLRDAGCDIVTITQYLRPSARHHPVERWVKPEEFVQFARFAEGLGFAGVLAGPLVRSSYRAGRLYEQARNSRALASR

Gene
lipA
Protein
Lipoyl synthase
Organism
Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.501 kDa
Sequence
MNAPASPAASPSQRARKPDWIRVKAPTSPGYAETRKLMRELNLHTVCEEAACPNIGECWTKKHATVMILGDTCTRACAFCNVKTGMPRPVDLLEPEHTAIAAAKMGLSHIVITSVDRDDLPDGGASQFVKVINALRRETPQTTIEILTPDFRNKPESAVAAIVDARPDVYNHNLETVPRLYPTIRPGARYYASLRLLESVKRRDPSIFTKSGIMLGLGEERMEVHQVMDDMRSADIDFMTMGQYLQPTPKHAKVIDFVTPQAFDAYAQIARAKGFLQVASSPLTRSSYHAGDDFEHMRAAREAQLARVRAD

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.695 kDa
Sequence
MTDSESPTPKKSIPARFPKWLRQKLPLGRVFAQTDNTIKNKGLPTVCEEASCPNRTHCWSRHTATYLALGDACTRRCGFCDIDFTRNPLPPDPEEGAKIAESAKALGLKHIVITMVSRDDLEDGGASALVHIIETLHTELPTATIEVLASDFEGNIAALHHLLDTHIAIYNHNVETVERLTPFVRHKATYRRSLMMLENAAKYLPNLMTKSGIMVGLGEQESEVKQTLKDLADHGVKIVTIGQYLRPSRRHIPVKSYVSPETFDYYRSVGESLGLFIYAGPFVRSSFNADSVFEAMRQRETSTSSLLPNKD

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.665 kDa
Sequence
MTDSESPTPKKSIPARFPKWLRQKLPLGRVFAQTDNTIKNKGLPTVCEEASCPNRTHCWSRHTATYLALGDACTRRCGFCDIDFTRNPLPPDPEEGAKIAESAKALGLKHIVITMVSRDDLEDGGASALVHIIETLHTELPTATIEVLASDFEGNIAALHHLLDAHIAIYNHNVETVERLTPFVRHKATYRRSLMMLENAAKYLPNLMTKSGIMVGLGEQESEVKQTLKDLADHGVKIVTIGQYLRPSRRHIPVKSYVSPETFDYYRSVGESLGLFIYAGPFVRSSFNADSVFEAMRQRETSTSSLLPNKD

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.695 kDa
Sequence
MTDSESPTPKKSIPARFPKWLRQKLPLGRVFAQTDNTIKNKGLPTVCEEASCPNRTHCWSRHTATYLALGDACTRRCGFCDIDFTRNPLPPDPEEGAKIAESAKALGLKHIVITMVSRDDLEDGGASALVHIIETLHTELPTATIEVLASDFEGNIAALHHLLDTHIAIYNHNVETVERLTPFVRHKATYRRSLMMLENAAKYLPNLMTKSGIMVGLGEQESEVKQTLKDLADHGVKIVTIGQYLRPSRRHIPVKSYVSPETFDYYRSVGESLGLFIYAGPFVRSSFNADSVFEAMRQRETSTSSLLPNKD

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.661 kDa
Sequence
MTDSESPIPKKSIPARFPKWLRQKLPLGRVFAQTDNTIKNKGLPTVCEEASCPNRTHCWSRHTATYLALGDACTRRCGFCDIDFTRNPLPPDPEEGAKIAESAKALGLKHIVITMVSRDDLEDGGASALVHIIETLHTELPTATIEVLASDFEGNIAALHHLLDAHIAIYNHNVETVERLTPFVRHKATYRRSLMMLENAAKYLPNLMTKSGIMVGLGEQESEVKQTLKDLADHGVKIVTIGQYLRPSRRHIPVKSYVSPETFDYYRSVGESLGLFIYAGPFVRSSFNADSVFEAMRQRETSTSALLPNKD

Gene
lipA
Protein
Lipoyl synthase
Organism
Thiobacillus denitrificans (strain ATCC 25259)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.174 kDa
Sequence
MADPLQHKGAAKTSRIPIKIVPQERQRLPPWIRAKAPSLPNVGRLKGILREAKLHTVCEEASCPNLGECFGHGTATFMILGDLCTRRCPFCDVGHGTPLPPDADEPRHLAETIALMALKYVVITSVDRDDLRDGGAGHFAECIAAVREKSPATRIEILTPDFRGRLDKALAALDRAPPDVMNHNLETVPRLYKAARPGADYAHSLKLLQDFRTRHPDIPTKSGLMLGLGETDDEILEVMRDLRAHGVDMLTLGQYLQPSRHHLAVLRFVTPERFAQFEQEALAMGFRHAACGPMVRSSYHADQQAAAAAAG

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.83 kDa
Sequence
MSSRRKPEWLKMRPPSGERFTDIKETLRDNDLHTVCEEASCPNMGECWSGRDGPGTATFMLMGDRCSRGCNFCDVKTGGMEPLDPDEPANVAESVAEIGLDYVVLTSVDRDDLDDQGAGHFARTIREIKERDPSILVEVLIPDFQGEKSLVQKIIDAGPDVIAHNIETVARRQVPVRDRRAGYEQSLSVLEYVTRESDIYTKTSIMLGVGEYDHEVYQTLGDLREAGVDVVTLGQYLQPSRSHLDVADYVHPQKFETWQRVAESEFGFLYCASGPMVRSSYKAGELFVDAVLREGKSVQEARRNARRAASE

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.83 kDa
Sequence
MSSRRKPEWLKMRPPSGERFTDIKETLRDNDLHTVCEEASCPNMGECWSGRDGPGTATFMLMGDRCSRGCNFCDVKTGGMEPLDPDEPANVAESVAEIGLDYVVLTSVDRDDLDDQGAGHFARTIREIKERDPSILVEVLIPDFQGEKSLVQKIIDAGPDVIAHNIETVARRQVPVRDRRAGYEQSLSVLEYVTRESDIYTKTSIMLGVGEYDHEVYQTLGDLREAGVDVVTLGQYLQPSRSHLDVADYVHPQKFETWQRVAESEFGFLYCASGPMVRSSYKAGELFVDAVLREGKSVQEARRNARRAASE

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.719 kDa
Sequence
MSVAAEGRRLLRLEVRNAQTPIERKPPWIKTRARIGPEYTELKNLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDRDEPRRVADSVRTMGLRYATVTGVARDDLPDGGAWLYAATVRAIKELNPSTGVELLIPDFNGEPTRLAEVFESGPEVLAHNVETVPRIFKRIRPAFTYRRSLGVLTAARDAGLVTKSNLILGLGETSDEVRTALGDLRDAGCDIVTITQYLRPSARHHPVERWVKPEEFVQFARFAEGLGFAGVLAGPLVRSSYRAGRLYEQARNSRALASR

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
311 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.719 kDa
Sequence
MSVAAEGRRLLRLEVRNAQTPIERKPPWIKTRARIGPEYTELKNLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDRDEPRRVADSVRTMGLRYATVTGVARDDLPDGGAWLYAATVRAIKELNPSTGVELLIPDFNGEPTRLAEVFESGPEVLAHNVETVPRIFKRIRPAFTYRRSLGVLTAARDAGLVTKSNLILGLGETSDEVRTALGDLRDAGCDIVTITQYLRPSARHHPVERWVKPEEFVQFARFAEGLGFAGVLAGPLVRSSYRAGRLYEQARNSRALASR

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlamydia abortus (strain DSM 27085 / S26/3)
Length
310 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.056 kDa
Sequence
MNDTPNDIQKPKQGKRFSERLPHWLRQALPKGSVFDFTDKTIKRTGMATVCEEALCPNRTRCWSRKTATYLALGDACSRRCGFCNIDFTKKPLPPDPDEPRKIAESAKILQLKHIVLTMVARDDLEDGGASCLVRIIDTLHKELPESTVEMLASDFQGNVDALHTLLDSGLTIYNHNVETVERLTPVVRHKATYRRSLFMLEQAALYLPDLKIKSGIMVGLGEQESEVKQTLKDLADHGVRIVTIGQYLRPSRLHIPVKSYVTPETFDYYRRVGESLGLFVYAGPFVRSSFNADIVLQDMENKQSKMAKT

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus carnosus (strain TM300)
Length
310 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.398 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLHTVCEEAKCPNIHECWGERRTATFMILGAVCTRACRFCAVKTGLPNELDLGEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPYTTIEILPSDMGGDYDALETLMASKPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEELHETMDDLRAADVDILTIGQYLQPSRKHLKVQKYYSPLEFGKLRKVAMEKGFKHCQAGPLVRSSYHADEQVNEAAKERQRIGDEKLEAAKNEA

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus carnosus (strain TM300)
Length
310 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.398 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLHTVCEEAKCPNIHECWGERRTATFMILGAVCTRACRFCAVKTGLPNELDLGEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPYTTIEILPSDMGGDYDALETLMASKPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEELHETMDDLRAADVDILTIGQYLQPSRKHLKVQKYYSPLEFGKLRKVAMEKGFKHCQAGPLVRSSYHADEQVNEAAKERQRIGDEKLEAAKNEA

Gene
lipA
Protein
Lipoyl synthase
Organism
Prochlorococcus marinus (strain MIT 9215)
Length
310 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.025 kDa
Sequence
MIKIYLDEADQSHLTSISKNAATKPEWLRVKAPQFERIGNTASLLSDLKLNTVCQEASCPNIGECFASGTATFLIMGPACTRACPYCDINFDRSKRDLDPTEPHRLAEAVSRMNLKHVVITSVNRDDLDDGGASQFFQCVSEVRKKSPETTIELLIPDLCGNWQALELVLDSKPNVLNHNIETVKSLYRKVRPQGNYQRTLDLLKRTKEYFPSVYTKSGFMLGLGESDDEVLNLLSDLKNHFVDIVTIGQYLSPGPKHLPVQRFVSPPKFTYFKLFGEDNLGFMQVVSSPLTRSSYHAEEIQKLMKKYPR

Gene
lipA
Protein
Lipoyl synthase
Organism
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Length
310 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.418 kDa
Sequence
MTNPAETARPERQRKPDWIRVKAPTSKGYGETRALMRELGLNTVCEEAACPNIGECWTKKHATVMILGDVCTRACAFCNVKTGMPRAVDPMEPINVATAAAKMGLEHIVITSVDRDDLPDGGAGHFVKVIKALRELTPNTTIEILTPDFRNKMEAAVESIVEAGPDVYNHNLETVPRLYPTIRPGARYYASLRLLEQVKRHDPRIFTKSGVMLGLGEERLEVHQVMDDMRSAQIDFLTMGQYLQPTPKHAKVIEFVTPKAFDAYGSIARAKGFLQVAASPLTRSSYHAGEDFRQMRQAREAQLAKAAQKA

Gene
lipA
Protein
Lipoyl synthase
Organism
Buchnera aphidicola subsp. Cinara cedri (strain Cc)
Length
310 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.523 kDa
Sequence
MLKEKKDKEKNIYMIPKILKSSKSKSILKKPKWLKIKLPSNLKKINKIKKILKKNFLHSVCEEANCPNLPECFNNGTATFMILGSICTRKCPFCAVTKGRAQKIDKNEPKKILDIVIKLKLTYVVLTSVARDDLKDGGAKHFSKCIYEIRKKKNIKVEILVPDFRGKEKIALKIFNKFPPDIFNHNIENVPRLYSLIRPGADYIKSLNLLYQFKKICPNIPTKSGLMLGLGEKKKEIISVLKDLKSVGVSIVTIGQYLQPSKNHLLVQKYITPKEFKNFEYIALSLGFSKVFCGPLVRSSYHADRQYLSF

Gene
lipA
Protein
Lipoyl synthase
Organism
Pelobacter carbinolicus (strain DSM 2380 / NBRC 103641 / GraBd1)
Length
309 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.154 kDa
Sequence
MDVGQKKRGADKTALATTDEQGALSKPTWIRAKAPISPEVGRLTGILRDLHLHTVCEEASCPNLGECFKRGTATFMIMGDVCTRRCPFCDVAHGRPAALDTEEPGHLADAIGAMKLKYVVITSVTRDDLEDGGAAHFAQCIESIRKKTEGVKVEILVPDFRGHVDAALKNLGNCLPDVFNHNLETVPRLYAESRPGARYHESLRLLQRFKETYPGIPTKSGLMLGLGETDEEILEVMRDLRVHGCDMLTIGQYLRPSRHHLPVQRYVTPEQFEAFRVAGLKMGFSQVASGPLVRSSYHADLQAKEVLHT

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus clausii (strain KSM-K16)
Length
309 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.375 kDa
Sequence
MPEKDEKEQHMRKPDWLKIKLNTNESYTGLKKMMREKKLHTVCEEARCPNIHECWAVRKTATFMILGDICTRGCRFCAVKTGLPTELDLQEPERVAESVETMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFCTIEVLPSDMLGNESSLQTLMDARPNIMNHNIETVRRLTPKVRARAKYDRTLEFLRRAKEMHPDIPTKSSLMVGLGETKEEILETMDDLRANNVDILTIGQYLQPTKKHLKVIKYYHPDEFAELKEIAMQKGFSHCEAGPLVRSSYHADEQVNQAQVNMEARKAQGEQQRV

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / NBRC 14720 / NCIMB 2260 / Gabara)
Length
309 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.323 kDa
Sequence
MSSRRRKPEWLRTRPPSGRRFTEIKETLRDRDLNTVCEEANCPNLGDCWSGRDGPGTATFMLLGDRCSRGCNFCDVATGGMDPLDPDEPANVAEAVAEIGLDYVVLTSVDRDDLDDGGAGHFAETIREIKRRDTSVLVEALIPDFQGDTDAVDRIIDADPDVVAHNVETVERLQWPVRDRRAGYEQSLDVLRQIAAADGCYAKTSLMLGVGEYAHEVYRTLGDLSEVGVDIVTFGQYLQPSRSHLEVFEYVTPDTFDVWKRVAETEFGFLYCASGPMVRSSFKAGELFVEALERDGLDIEAARAAAERQ

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlamydia muridarum (strain MoPn / Nigg)
Length
308 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.278 kDa
Sequence
MSNSPESSTPKQSIPARFPKWLRQKLPLGKVFSRTDGTIKNKGLPTVCEEASCPNRTHCWSRHTATYLALGDACTRRCGFCDIDFTKKPLPPDPQEGEKIAASAKALGLKHIVITMVSRDDLEDGGADALARIITTLHIELPEATIEVLASDFEGNIDALHHLLDARIAIYNHNVETVERLSPLVRHKATYRRSLMMLEQAAQYLPDLMIKSGIMVGLGEQESEIKQTLKDLADHGVKIVTIGQYLRPSRRHIPVKSYVSPETFDYYRSVGEALGLFIYAGPFVRSSFNADAVFEAMSQRERLSASIQ

Gene
lipA
Protein
Lipoyl synthase
Organism
Pelagibacter ubique (strain HTCC1062)
Length
308 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.15 kDa
Sequence
MTTKPRHPEKVNKPLNPIKKKPDWIRSKLVNSKEFFLTKTIVNNNNLVTVCQEANCPNITECWSKRHATFMIMGDTCTRACAFCDVKTGRPGKLDSLEPVKIAEAVKKLNLKHVVITSVDRDDLDDGGSNHFFEVIDQTRKRNPNTSIEVLTPDFLRKGDAYKKVLEANPDVFNHNIETVPRLYLKVRPGSRYFSSLELLKNAKLVNKNVFTKSGLMVGLGENKEEIIQVMDDLKAADVDFLTIGQYLQPSVRHHPLDRYYHPDEFKELETIAKSKGFLLVSSTPLTRSSYHADEDFAKLQLNRINNH

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium avium (strain 104)
Length
307 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.532 kDa
Sequence
MTVAPEGRKLLRLEVRNADTPIERKPPWIRVRARMGPEYTELKSLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDRDEPRRVADSVRTMGLRYATVTGVARDDLPDGGAWLYAETVRAIKELNPSTGVELLIPDFNGRPDRLAEVFGSRPEVLAHNVETVPRIFKRIRPAFTYRRSLDVLTAAREAGLVTKSNLILGLGETPDEVRTALADLRGAGCDIITITQYLRPSARHHPVERWVKPEEFVEFARHAEELGFSGVLAGPLVRSSYRAGRLYRQAARARA

Gene
lipA
Protein
Lipoyl synthase
Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Length
307 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.576 kDa
Sequence
MTVAPEGRKLLRLEVRNAETPIERKPPWIRVRARMGPEYTELKSLVRREGLHTVCEEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPAELDRDEPRRVADSVRTMGLRYATVTGVARDDLPDGGAWLYAETVRAIKELNPSTGVELLIPDFNGRPDRLAEVFGSRPEVLAHNVETVPRIFKRIRPAFTYRRSLDVLTAAREAGLVTKSNLILGLGETPDEVRTALADLRGAGCDIITITQYLRPSARHHPVERWVKPEEFVEFARHAEELGFSGVLAGPLVRSSYRAGRLYRQTARARA

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlamydia pneumoniae
Length
307 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.993 kDa
Sequence
MKCRPTLNTDQPRVRKKLPERFPKWLQRPLPQGSAFHATDATIKRSGMPTVCEEALCPNRAECWSRKTATYLALGDVCTRSCGFCNIGHSKTPPALDPTEPERIALSAKELGLKHVVITMVARDDLEDGGAQGLVDIIQKLREELPQATTEVLASDFQGNVSALHTLLDSGITIYNHNVETVARLSPLVRHKATYARSMFMLEQAANYLPDLKIKSGIMVGLGEMEGEVKQTLQDLASIGVRIVTIGQYLRPSRKHLQVKSYVTPETFDYYRRVGEAMGLFVYAGPFVRSSFNADMILASVQDKASA

Gene
lipA
Protein
Lipoyl synthase
Organism
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Length
306 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.2 kDa
Sequence
MAELIPLNEVGVAQPASGAVNRPRRPEWLKARAPGGVNYHDVLRLMREKNLHTVCEEARCPNIGECWNHRTATFLLLGDICTRGCRYCAIGKGKPKPIDENEPERVAESVAHLKLKFAVLTSVNRDDVPDGGAHIFARTIELIRQKVPDCKVEVLIPDFDGNWDALATVLAAEPDVLNHNIETVPRLFRRFRPRAKFEQSIELLARARAARPKLVTKSGMMVGAGETNEEVYEVIDRLRSVDVNVLTIGQYLAPDASYWPVHRYVTPAEFAEFRSYALARGFTHVESGPLVRSSYNAHLHVGAAQH

Gene
lipA
Protein
Lipoyl synthase
Organism
Chloroflexus aggregans (strain MD-66 / DSM 9485)
Length
306 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.453 kDa
Sequence
MSELIPLSEVGVVNPTSATTNRPRRPEWLKARAPGGVNYHDVLRLMREKNLHTVCEEARCPNIGECWNHRTATFLLLGDICTRGCRYCAIGKGKPKPIDEEEPERVAESVAHLRLKFAVLTSVNRDDVPDGGAHIFARTIELIRQKVPDCKVEVLIPDFDGNWDALAMVLDAEPDVLNHNIETVPRLFRRFRPRAKFEQSIELLARARAAHPHLVTKSGMMVGAGETNEEVYEVIDRLREVDVNVLTIGQYLAPDASYWPVHRYVTPAEFADFRAYALARGFRHVESGPLVRSSYNAHLHVGAAQH

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Length
306 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.469 kDa
Sequence
MNPLKKKPRSKNLNPTVPLPDWMKVRVSFPTDSDALSVVRAEVESKELHTVCESASCPNLNHCWNRKTATYMLAGDICTRRCQYCDVAFGKPKPLDSLEPERVARSVQSLGLRHVVLTAVNRDDLKDGGASHFAETITKIKTYHKDCTIEVLIPDFKAKEDSLQILYAAKPNIINHNIETVESLFPTITPQKNYKRSLEVLAHIANHGFLTKSGIILGLGETDEDVNQCLMDLFAHGVRMLTIGQYLQPGPTHYPVQSFVRPETFVMWKETAYKIGFKTVASGPLVRSSYHADEYFHEESQILPTE

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Length
306 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.469 kDa
Sequence
MNPLKKKPRSKNLNPTVPLPDWMKVRVSFPTDSDALSVVRAEVESKELHTVCESASCPNLNHCWNRKTATYMLAGDICTRRCQYCDVAFGKPKPLDSLEPERVARSVQSLGLRHVVLTAVNRDDLKDGGASHFAETITKIKTYHKDCTIEVLIPDFKAKEDSLQILYAAKPNIINHNIETVESLFPTITPQKNYKRSLEVLAHIANHGFLTKSGIILGLGETDEDVNQCLMDLFAHGVRMLTIGQYLQPGPTHYPVQSFVRPETFVMWKETAYKIGFKTVASGPLVRSSYHADEYFHEESQILPTE

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus haemolyticus (strain JCSC1435)
Length
306 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.161 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYIGLKKMMREKNLHTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYEALETLMASKPDILNHNIETVRRLTPRVRARATYERTLEFLRRSKELQPDIPTKSSLMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVEKYYTPLEFGKLRKVAMDKGFKHCEAGPMVRSSYHADEQVNEAAKEKHRLGEEKLQQN

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Length
306 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.469 kDa
Sequence
MNPLKKKPRSKNLNPTVPLPDWMKVRVSFPTDSDALSVVRAEVESKELHTVCESASCPNLNHCWNRKTATYMLAGDICTRRCQYCDVAFGKPKPLDSLEPERVARSVQSLGLRHVVLTAVNRDDLKDGGASHFAETITKIKTYHKDCTIEVLIPDFKAKEDSLQILYAAKPNIINHNIETVESLFPTITPQKNYKRSLEVLAHIANHGFLTKSGIILGLGETDEDVNQCLMDLFAHGVRMLTIGQYLQPGPTHYPVQSFVRPETFVMWKETAYKIGFKTVASGPLVRSSYHADEYFHEESQILPTE

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Length
306 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.469 kDa
Sequence
MNPLKKKPRSKNLNPTVPLPDWMKVRVSFPTDSDALSVVRAEVESKELHTVCESASCPNLNHCWNRKTATYMLAGDICTRRCQYCDVAFGKPKPLDSLEPERVARSVQSLGLRHVVLTAVNRDDLKDGGASHFAETITKIKTYHKDCTIEVLIPDFKAKEDSLQILYAAKPNIINHNIETVESLFPTITPQKNYKRSLEVLAHIANHGFLTKSGIILGLGETDEDVNQCLMDLFAHGVRMLTIGQYLQPGPTHYPVQSFVRPETFVMWKETAYKIGFKTVASGPLVRSSYHADEYFHEESQILPTE

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus haemolyticus (strain JCSC1435)
Length
306 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.161 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYIGLKKMMREKNLHTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYEALETLMASKPDILNHNIETVRRLTPRVRARATYERTLEFLRRSKELQPDIPTKSSLMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVEKYYTPLEFGKLRKVAMDKGFKHCEAGPMVRSSYHADEQVNEAAKEKHRLGEEKLQQN

Gene
lipA
Protein
Lipoyl synthase
Organism
Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)
Length
306 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.2 kDa
Sequence
MAELIPLNEVGVAQPASGAVNRPRRPEWLKARAPGGVNYHDVLRLMREKNLHTVCEEARCPNIGECWNHRTATFLLLGDICTRGCRYCAIGKGKPKPIDENEPERVAESVAHLKLKFAVLTSVNRDDVPDGGAHIFARTIELIRQKVPDCKVEVLIPDFDGNWDALATVLAAEPDVLNHNIETVPRLFRRFRPRAKFEQSIELLARARAARPKLVTKSGMMVGAGETNEEVYEVIDRLRSVDVNVLTIGQYLAPDASYWPVHRYVTPAEFAEFRSYALARGFTHVESGPLVRSSYNAHLHVGAAQH

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain JH1)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain USA300)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain NCTC 8325)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain JH9)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.884 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMRKKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain COL)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain Newman)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain N315)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain MRSA252)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain MSSA476)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain USA300 / TCH1516)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain MW2)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain JH1)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain USA300)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain NCTC 8325)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain JH9)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.884 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMRKKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain COL)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain Newman)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain N315)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain MRSA252)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain MSSA476)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain USA300 / TCH1516)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus aureus (strain MW2)
Length
305 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.885 kDa
Sequence
MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Koribacter versatilis (strain Ellin345)
Length
304 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.312 kDa
Sequence
MAPELIQIDLEPRKPAPKPSWLRAKAPMGENYHDLKKLARGMNLHTVCESAQCPNIGECWNHKTATFMLLGNLCTRRCGFCAVPKGRPEPIDFDEPRRVAEAVATLGLNFAVVTSVNRDDDNVGAAQVFAQTIEQIREQKPGCRVEVLIPDFQGNDESLRIVLAAKPEILNHNTETVPRLYRAVRSGARYERTLNLLRRAKEINPAQVTKTGVMVGLGETTEELLHVYRDLARQNVDILTIGQYLRPSKDHAPMTRYYTPEEFLFMKEEAMKMGFRHVESGPLVRSSYHAHEQANSTKQPLVTI

Gene
lipA
Protein
Lipoyl synthase
Organism
Macrococcus caseolyticus (strain JCSC5402)
Length
304 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.754 kDa
Sequence
MATKNEEILRKPEWLKIKLNTNKSYTGLKKMMREHNLNTVCEEAKCPNIHECWGERKTATIMILGAICTRACRFCAVKTGLPNELDLNEPERVAESVRLMNLKHVVITAVARDDLKDGGAHVYAETIRKVREVNPYTTIEVLPSDMGGSIENWETLMAAKPDILNHNIETVRRLTPRVRARATYDRSLEVLRRSKELYPDIPTKSSLMVGLGETTEEIYEVMDDLRANDVDIMTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMEKGFKHCQAGPMVRSSYHADEQVNEAAKEKHRLGELSSK

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Length
304 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.028 kDa
Sequence
MATRNEEILRKPDWLKIKLNTNDNYTGLKKMMREKNLHTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDQGSNVYAETVRKVRERNPFTTIEILPSDMGGDYEALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLQFLRRSKELQPDIPTKSSLMVGLGETMEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVEKYYTPLEFGKMRKIAMEKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEEQLN

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Length
304 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.028 kDa
Sequence
MATRNEEILRKPDWLKIKLNTNDNYTGLKKMMREKNLHTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDQGSNVYAETVRKVRERNPFTTIEILPSDMGGDYEALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLQFLRRSKELQPDIPTKSSLMVGLGETMEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVEKYYTPLEFGKMRKIAMEKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEEQLN

Gene
lipA
Protein
Lipoyl synthase
Organism
Macrococcus caseolyticus (strain JCSC5402)
Length
304 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.754 kDa
Sequence
MATKNEEILRKPEWLKIKLNTNKSYTGLKKMMREHNLNTVCEEAKCPNIHECWGERKTATIMILGAICTRACRFCAVKTGLPNELDLNEPERVAESVRLMNLKHVVITAVARDDLKDGGAHVYAETIRKVREVNPYTTIEVLPSDMGGSIENWETLMAAKPDILNHNIETVRRLTPRVRARATYDRSLEVLRRSKELYPDIPTKSSLMVGLGETTEEIYEVMDDLRANDVDIMTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMEKGFKHCQAGPMVRSSYHADEQVNEAAKEKHRLGELSSK

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Length
304 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.028 kDa
Sequence
MATRNEEILRKPDWLKIKLNTNDNYTGLKKMMREKNLHTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDQGSNVYAETVRKVRERNPFTTIEILPSDMGGDYEALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLQFLRRSKELQPDIPTKSSLMVGLGETMEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVEKYYTPLEFGKMRKIAMEKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEEQLN

Gene
lipA
Protein
Lipoyl synthase
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Length
304 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
35.028 kDa
Sequence
MATRNEEILRKPDWLKIKLNTNDNYTGLKKMMREKNLHTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDQGSNVYAETVRKVRERNPFTTIEILPSDMGGDYEALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLQFLRRSKELQPDIPTKSSLMVGLGETMEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVEKYYTPLEFGKMRKIAMEKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEEQLN

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia bellii (strain OSU 85-389)
Length
303 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.256 kDa
Sequence
MSKRPDWIKVKAPNSSEYYNTKDLIKNLKLNTVCEEAACPNIGECWSKKHATVMILGSVCTRACRFCNVKTGRPDLLDPHEPQRLAEAVQKLGLKHVVITSVDRDDLEDGGATHFAECISEIRKSSPNTTIEILTPDFLRKDGAAEIIANAKPDVFNHNVETVPSLYNTIRPGARYYNSLSLLHNIKKLSPEVFTKSGMMVGLGEEISEVVQVMDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERVARTKGFLMVSASPLTRSSYHADEDFEKLKENYRHRHCEERRSIDVAIS

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Length
303 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.887 kDa
Sequence
MNIHRKPEWLRKKINPAAHGAMDELLGELRLHTVCREARCPNITECFRERQATFLILGAECTRLCSFCNVTKGEPLPPDPDEPARVAQAVVRLSLAHVVITSPTRDDLPDGGAGHYVATVATIGRVAPATVVELLIPDFLGSRAALADVVAAAPRIIGHNVETVPRLYAIRAGADYGRSLAVLRTLRELAPGCATKSGLMLGLGETEEEVLAVMADLRRVDCTYLSLGQYLAPSRFHHPVREFVLPETFDRLKELAEKMGFRHVESGPYVRSSYHAAGYGGGTRTDQPVASGCLSDQEGVSAQ

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Length
303 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.533 kDa
Sequence
MAKKEEYVRKPDWLKIKLNTNETYTGLKKMMREKNLHTVCEEAKCPNIHECWAVRKTATFMILGDVCTRACRFCAVKTGLPNELDLQEPERVAESVEIMGLKHAVITAVARDDLKDGGAGVFAETVRAVRRRNPFCTIEVLPSDMMGNDDNLKTLMDARPNILNHNIETVRRLTPRVRARATYERSLEFLRRAKEMQPDIPTKSSLMIGLGETKDEIIETMDDLRANNVDIMTIGQYLQPTKKHLKVQKYYHPDEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVNEAQVREEARKAAAKS

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197)
Length
302 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.783 kDa
Sequence
MINPLKKKPRTHFLQKAPEKPDWLKVKLTFPDPKNNPVAIVRNSLEKKKLNTVCESASCPNLNHCWSRKTATYMLGGDICTRRCSYCDVASGKPSALDRDEPKRVAESAIALGLKHVVITAVNRDDLEDGGAAHFAETVEVVREGLPDCKIELLVPDFKVRPESLEIIFQCKPDIFNHNVETIKRLFPEVAPQKKYERSLDVLKIASEKGFLTKSGLILGMGETVEEVKECMRDLIGVGVSLLTLGQYLQPTPTHLPVKSYVLPEVFQELRIYGKSIGFKGVFSGPLVRSSYHADEQVSWNP

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain L550)
Length
302 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.783 kDa
Sequence
MINPLKKKPRTHFLQKAPEKPDWLKVKLTFPDPKNNPVAIVRNSLEKKKLNTVCESASCPNLNHCWSRKTATYMLGGDICTRRCSYCDVASGKPSALDRDEPKRVAESAIALGLKHVVITAVNRDDLEDGGAAHFAETVEVVREGLPDCKIELLVPDFKVRPESLEIIFQCKPDIFNHNVETIKRLFPEVAPQKKYERSLDVLKIASEKGFLTKSGLILGMGETVEEVKECMRDLIGVGVSLLTLGQYLQPTPTHLPVKSYVLPEVFQELRIYGKSIGFKGVFSGPLVRSSYHADEQVSWNP

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197)
Length
302 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.783 kDa
Sequence
MINPLKKKPRTHFLQKAPEKPDWLKVKLTFPDPKNNPVAIVRNSLEKKKLNTVCESASCPNLNHCWSRKTATYMLGGDICTRRCSYCDVASGKPSALDRDEPKRVAESAIALGLKHVVITAVNRDDLEDGGAAHFAETVEVVREGLPDCKIELLVPDFKVRPESLEIIFQCKPDIFNHNVETIKRLFPEVAPQKKYERSLDVLKIASEKGFLTKSGLILGMGETVEEVKECMRDLIGVGVSLLTLGQYLQPTPTHLPVKSYVLPEVFQELRIYGKSIGFKGVFSGPLVRSSYHADEQVSWNP

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain L550)
Length
302 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.783 kDa
Sequence
MINPLKKKPRTHFLQKAPEKPDWLKVKLTFPDPKNNPVAIVRNSLEKKKLNTVCESASCPNLNHCWSRKTATYMLGGDICTRRCSYCDVASGKPSALDRDEPKRVAESAIALGLKHVVITAVNRDDLEDGGAAHFAETVEVVREGLPDCKIELLVPDFKVRPESLEIIFQCKPDIFNHNVETIKRLFPEVAPQKKYERSLDVLKIASEKGFLTKSGLILGMGETVEEVKECMRDLIGVGVSLLTLGQYLQPTPTHLPVKSYVLPEVFQELRIYGKSIGFKGVFSGPLVRSSYHADEQVSWNP

Gene
lipA
Protein
Lipoyl synthase
Organism
Orientia tsutsugamushi (strain Boryong)
Length
302 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.099 kDa
Sequence
MCSDKNITATALVRPSWLRVKAPFSDEYQSTNELIKSLKLNTVCKEAACPNIGECWSKKHATVMILGSICTRACAFCNVSTGKPEQVDEYEPYRLSEAVMKLGLKHVVITSVDRDDLSDGGASHFAKCITYIRERSPTTSIEVLTPDFLRKHEAWKIVAKARPDVYNHNIETVPSLYLKVRPGARYYNSLNLLHQVKIFDSSIFTKSGIMVGLGETKHEVLQVMDDLRAAEVDFLTIGQYLRPSARHIDVGRYVTPDEFDYYAKVARSKGFLMVSASPLTRSSYHAGEHFEKLKQMRLQNII

Gene
lipA
Protein
Lipoyl synthase
Organism
Orientia tsutsugamushi (strain Ikeda)
Length
302 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.099 kDa
Sequence
MCSDKNITATALVRPSWLRVKAPFSDEYQSTNELIKSLKLNTVCKEAACPNIGECWSKKHATVMILGSICTRACAFCNVSTGKPEQVDEYEPYRLSEAVMKLGLKHVVITSVDRDDISDGGASHFAKCITYIRERSPSTSIEVLTPDFLRKHDAWKIVAKARPDVYNHNIETVPSLYLKVRPGARYYNSLNLLHQVKIFDSSIFTKSGIMVGLGETKHEVLQVMDDLRAAEVDFLTIGQYLRPSARHIDVDRYVAPDEFDYYARVAKSKGFLMVSASPLTRSSYHAGEHFEKLKQMRLQNII

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
Length
301 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.126 kDa
Sequence
MSNLNKRPDWIKVKAPNSAEYYNTKDLIKNLRLNTVCEEAACPNIGECWSKKHATVMILGSVCTRACRFCNVKTGRPDLLDPHEPQRLAEAVQKLNLKHVVITSVDRDDLDDGGATHFAECISEIRKSSPNTTIEILTPDFLRKEGAAEIIANAKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEISEVIQVMDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERIARTKGFLMVSATPLTRSSYHADEDFQKLKENYQQRHCEEAWPA

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Length
301 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.666 kDa
Sequence
MNPLKKKPRTHSLQNAPEKPDWLKVKLAFPDPKNNPVAIVRNSLEEKKLNTVCESASCPNLNHCWSRKTATYMLGGDICTRRCSYCDVASGKPFPLDPEEPKRIAESSIALGLRHVVITSVNRDDLEDGGAAHFAKTVKEIRKGLPDCKIELLIPDLKVKQEALEIIFECNPDIFNHNLETVKRLFPEVAPQKRYERSLDVLKIASARGFLTKSGLILGMGETLEEVKECMQDLASVGVSLLTLGQYLQPTSTHLPVKEYVVPQVFKDLRIYGKSIGFKGVFSGPLVRSSYHADEQISWNP

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Length
301 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.724 kDa
Sequence
MNPLKKKPRTHSLQNAPEKPDWLKVKLAFPDPKNNPVAIVRNSLEEKKLNTVCESASCPNLNHCWSRKTATYMLGGDICTRRCSYCDVASGKPFPLDPEEPKRIAESSIALDLRHVVITSVNRDDLEDGGAAHFAKTVKEIRKGLPDCKIELLIPDLKVKQEALEIIFECNPDIFNHNLETVKRLFPEVAPQKRYERSLDVLKIASARGFLTKSGLILGMGETLEEVKECMQDLASVGVSLLTLGQYLQPTSTHLPVKEYVVPQVFKDLRIYGKSIGFKGVFSGPLVRSSYHADEQISWNP

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Length
301 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.666 kDa
Sequence
MNPLKKKPRTHSLQNAPEKPDWLKVKLAFPDPKNNPVAIVRNSLEEKKLNTVCESASCPNLNHCWSRKTATYMLGGDICTRRCSYCDVASGKPFPLDPEEPKRIAESSIALGLRHVVITSVNRDDLEDGGAAHFAKTVKEIRKGLPDCKIELLIPDLKVKQEALEIIFECNPDIFNHNLETVKRLFPEVAPQKRYERSLDVLKIASARGFLTKSGLILGMGETLEEVKECMQDLASVGVSLLTLGQYLQPTSTHLPVKEYVVPQVFKDLRIYGKSIGFKGVFSGPLVRSSYHADEQISWNP

Gene
lipA
Protein
Lipoyl synthase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Length
301 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.724 kDa
Sequence
MNPLKKKPRTHSLQNAPEKPDWLKVKLAFPDPKNNPVAIVRNSLEEKKLNTVCESASCPNLNHCWSRKTATYMLGGDICTRRCSYCDVASGKPFPLDPEEPKRIAESSIALDLRHVVITSVNRDDLEDGGAAHFAKTVKEIRKGLPDCKIELLIPDLKVKQEALEIIFECNPDIFNHNLETVKRLFPEVAPQKRYERSLDVLKIASARGFLTKSGLILGMGETLEEVKECMQDLASVGVSLLTLGQYLQPTSTHLPVKEYVVPQVFKDLRIYGKSIGFKGVFSGPLVRSSYHADEQISWNP

Gene
lipA
Protein
Lipoyl synthase
Organism
Roseiflexus sp. (strain RS-1)
Length
301 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.084 kDa
Sequence
MADLIPLIATDSLPSNRARRPEWLKVRAPGGANYHDVFRLMREQNLHTVCEEAHCPNIGECWNHRTATFLLLGNICTRGCRYCAIGKGKPEPIDEHEPERVAASVAHLKLKFAVLTSVNRDDVPDGGASIFARTIELIRQKAPDCKVEVLIPDFDGNWEALETVLAAEPDVLNHNIETVPRLFRRFRPRARFEQSIELLARARAARPYLVTKSGMMVGAGETNEEVYQVIDRLRDVDVNVLTIGQYLSPGASYWPVDRYVTPAEFAEFRRYALERGFRHVESGPLVRSSYHAHLHVNAQQH

Gene
lipA
Protein
Lipoyl synthase
Organism
Ehrlichia canis (strain Jake)
Length
299 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.985 kDa
Sequence
MRSKPDWLKVKMPTGDTFYQMRNLMKLYKLNTVCEEAACPNVGECWNKKHATVMILGSTCTRACAFCNVATGIPDKLDPHEPQNLAKAINSLKLHHVVITSVDRDDLPDGGAGHFVECIEEIRKRDDNITIEILTPDFLNKHGAIDKIAAVAPDVYNHNVETVPRLYARIRPKARYFHSLYLLKAVKYKNPKIFTKSGIMVGLGETKEEIYQVMDDLRSADVDFITIGQYLQPTPKHAVVDRYVTPEEFDHYKYVAYSKGFLMVASGPLVRSSYHAEEDFQKLKQNRTAMLMRAESNSI

Gene
lipA
Protein
Lipoyl synthase
Organism
Desulfotalea psychrophila (strain LSv54 / DSM 12343)
Length
299 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.578 kDa
Sequence
MACSHQKNEQMRVGKPKWLRRSLPTGPEYEKIRTLLKGSGLTTVCQEAQCPNQFECYSKGTATFMIMGDHCTRNCRFCAVAHGPKALPDEDEAERVADAVSLLGLRYAVITSVTRDDLADGGASCFVRVIEAIRKKNPKTLIEVLIPDLAGNWGALQTILDARPDVLNHNIETVPRLYSVARPGAEYRRSLELLREVRRRAPQMVTKTGMMLGLGEETEELYATWQDLRESDCDILTMGQYLQPTVDHLLVQRFVEPTEFDRLGDVALAKDFLAVASGPFVRSSYEAEKLFRKAELARK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus anthracis (strain A0248)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.701 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSNRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus anthracis (strain CDC 684 / NRRL 3495)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.701 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSNRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus thuringiensis (strain Al Hakam)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.702 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSDRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus anthracis
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.701 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSNRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cereus (strain AH820)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.701 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSNRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacillus kaustophilus (strain HTA426)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.056 kDa
Sequence
MATKEEHVRKPDWLKIKLNTNENYIGLKKLMRENRLHTVCEEAKCPNIHECWAVRRTATFMILGSVCTRACRFCAVKTGLPTELDWQEPERVAESVRIMNLKHVVVTAVARDDLKDGGAAVFAETVRAIRRKNPFTTIEVLPSDMGGVYENLKILMDARPDILNHNIETVRRLTPRVRARATYERSLEFLRRAKELQPDIPTKSSIMVGLGETKEEIIEAMDDLRANHVDILTIGQYLQPTKKHLKVVKYYHPDEFQELKEIALSKGFSHCEAGPLVRSSYHADEQVSEAAKARQLKA

Gene
lipA
Protein
Lipoyl synthase
Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.017 kDa
Sequence
MSSPDNSSPSLRIPPWLRVKLPCSHTFADTRALVEGLGLNTVCNSAKCPNMFECFSSGTATFLILGNVCTRNCAFCNITPGHVSPPDPDEPRRVAEAAARLALRHVVVTSVTRDDLDDGGAAHFAATITRLRAALPAATVEVLIPDFRGDHAALRTVMAAAPHIVNHNVETPPAHYARIRPQADYRQSLELLRRVKAAGGVAKSGLMVGLGENDTEVEGVLADLADCGCDIVTIGQYMRPSRQHPPVERYVHPDTFESFAACGRGMGIPFVFSAPLVRSSYNAESAYNALCTLRTEPA

Gene
lipA
Protein
Lipoyl synthase
Organism
Desulfovibrio vulgaris subsp. vulgaris (strain DP4)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.058 kDa
Sequence
MSSPDNSSPSLRIPPWLRVKLPCSHTFADTRALVEGLGLNTVCNSAKCPNMFECFSSGTATFLILGNVCTRNCAFCNITPGHVSPPDPDEPRRVAEAAARLALRHVVVTSVTRDDLDDGGAAHFAATITRLRAALPAATVEVLIPDFRGDHAALRTVMAAAPHIVNHNVETPPAHYARIRPQADYRQSLELLRRVKAAGGVAKSGLMVGLGENDTEVEGVLADLADCGCDIVTVGQYMRPSRQHPPVERYVHPDTFESFAACGRGMGIPFVFSAPLVRSSYNAESAYNALCTLRRKPA

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cereus (strain ATCC 10987 / NRS 248)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.688 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSDRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKENTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cereus (strain G9842)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.715 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMAGVEENLKMLMDAKPDILNHNIETVRRLSNRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVIKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cereus (strain 03BB102)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.702 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSDRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cereus (strain B4264)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.716 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSDRVRARAKYERSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cereus (strain AH187)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.688 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSDRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKENTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.786 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKQLHTVCEEAKCPNIHECWAVRKTATFMILGAICTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLRILMDAKPDILNHNIETVRRLSDRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLLEAMDDLRANNVDILTLGQYLQPSKKHLPVIRYYTPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKENTVEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cereus (strain Q1)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.688 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSDRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKENTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cereus (strain ZK / E33L)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.688 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSDRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKENTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.701 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSNRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus pumilus (strain SAFR-032)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.817 kDa
Sequence
MAKKEEHVRKPDWLKIKLNTNENYTGLKKMMRENNLNTVCEEAKCPNIHECWAVRRTATFMILGSVCTRACRFCAVKTGLPTELDLQEPERVADSVALMNLKHAVITAVARDDQKDGGAGVFAETVRAIRRKSPFTTIEVLPSDMGGNYDNLKTLMDTRPDILNHNIETVRRLTPRVRARATYDRSLEFLRRAKEMQPDIPTKSSIMIGLGETKEEIIEVMDDLLANNVDIMAIGQYLQPSKKHLKVQKYYHPDEFAELKEIAMAKGFSHCEAGPLVRSSYHADEQVNEASKKRQAQA

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus subtilis (strain 168)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.921 kDa
Sequence
MAKKDEHLRKPEWLKIKLNTNENYTGLKKLMRENNLHTVCEEAKCPNIHECWAVRRTATFMILGSVCTRACRFCAVKTGLPTELDLQEPERVADSVALMNLKHAVITAVARDDQKDGGAGIFAETVRAIRRKSPFTTIEVLPSDMGGNYDNLKTLMDTRPDILNHNIETVRRLTPRVRARATYDRSLEFLRRAKEMQPDIPTKSSIMIGLGETKEEIIEVMDDLLANNVDIMAIGQYLQPTKKHLKVQKYYHPDEFAELKEIAMQKGFSHCEAGPLVRSSYHADEQVNEASKKRQAQA

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.893 kDa
Sequence
MAKKDEHLRKPEWLKIKLNTNENYTGLKKLMRENNLHTVCEEAKCPNIHECWAVRRTATFMILGSVCTRACRFCAVKTGLPTELDLQEPERVADSVALMNLKHAVITAVARDDQKDGGAGVFAETVRAIRRKSPFTTIEVLPSDMGGNYDNLKTLMDTRPDILNHNIETVRRLTPRVRARATYDRSLEFLRRAKEMQPDIPTKSSIMIGLGETKEEIIEVMDDLLANNVDIMAIGQYLQPSKKHLKVQKYYHPDEFAELKEIAMQKGFSHCEAGPLVRSSYHADEQVNEASKKRQAQA

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus weihenstephanensis (strain KBAB4)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.716 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRENPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSNRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMLGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVIKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacillus sp. (strain WCH70)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.061 kDa
Sequence
MATNEEHLRKPEWLKIKLNTNENYTGLKKLMRENRLHTVCEEAKCPNIHECWAVRRTATFMILGNVCTRACRFCAVKTGLPTELDWQEPERVAESVRLMNLKHVVVTAVARDDLKDGGAAVFAETVRAIRRKNPFTTIEVLPSDMGGVYENLKTLMDARPDILNHNIETVRRLTPRVRARATYERSLEFLRRAKELQPDIPTKSSIMVGLGETKEEIIEAMDDLRANHVDILTIGQYLQPTKKHLKVVKYYHPDEFRELKEIALSKGFTHCEAGPLVRSSYHADEQVNAASAARQMKA

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacillus thermodenitrificans (strain NG80-2)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
34.096 kDa
Sequence
MATKEEHVRKPDWLKIKLNTNEHYTGLKKLMRENRLHTVCEEAKCPNIHECWAVRRTATFMILGSVCTRACRFCAVKTGLPTELDWQEPERVAESVRIMNLKHVVVTAVARDDLKDGGAAVFAETVRAIRRKNPFTTIEVLPSDMGGVYENLKTLMDARPDILNHNIETVRRLTPRVRARATYERSLEFLRRAKELQPDIPTKSSIMIGLGETKEEIIEAMDDLRANHVDILTIGQYLQPTKKHLKVVKYYHPDEFQELKEIALSKGFSHCEAGPLVRSSYHADEQVNEAAKARQLKA

Gene
lipA
Protein
Lipoyl synthase
Organism
Myxococcus xanthus (strain DK 1622)
Length
298 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.737 kDa
Sequence
MTETTRKPEWLKVRLPHGEGYERVKAIVKRTKLATVCEEARCPNIAECWGGGTATVMLMGEVCTRACRFCHVKVGAPPPLDPMEPIHLAQAVKEMDLEYIVVTSVNRDDRPDGGASHFASAIRELRRESPRTIVEVLIPDFKGVEKDLTTVAEAKPHVVAHNVETVERLTPTVRDRRAKYHQSLRVLEYLKNRPEGLYTKTSVMVGLGETDAELEQTFKDLRDVGVDVLTLGQYLQPSQYHLRVERFVTPAQFEAYKTLAESYGFLYVASGPLVRSSYRAAEFFMKGLMERERLERLG

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia akari (strain Hartford)
Length
297 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.492 kDa
Sequence
MTNLNKKPDWIKVKAPNSAEYYNTKDLIKNLSLNTVCEEAACPNIGECWSKKHATMIILGSVCTRACMFCNVKTGRPDLLDPHEPQRLAEAVQKLNLKHVVITSVDRDDLEDGGASHFAECINEIRKSSTNTTIEILTPDFLRKEGAAEIIANSKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEINEVVQVMDDLREAQVDFLTIGQYLQPTKNHAEVAKYVTPEEFQYLGRIAKTKGFLMVSSTPLTRSSYHADEDFQKLKENYQQRHTVA

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia prowazekii (strain Madrid E)
Length
297 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.711 kDa
Sequence
MTNLNKRPDWIKVKAPNSVEYYQTKDLIKNLRLNTVCEEAACPNIGDCWSRKHATVMILGAVCTRACRFCNVKTGRPDLLDPHEPRRLAEAVQKLNLQHVVITSVDRDDLEDGGASHFAECINEIRRSSPNTTIEILTPDFLRKEGAVEIIANAKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEINEVVQVMDDLREANVDFLTIGQYLQPTKSHAEIRKYVTPEEFKYLERIAKTKGFLMVSATPLTRSSYHADKDFQKLKGNYNIRLASM

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia typhi (strain ATCC VR-144 / Wilmington)
Length
297 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.658 kDa
Sequence
MTNVNRRPDWIKVKAPNSAEYYNTKDLIKNLRLNTVCEEAACPNIGECWSRKHATVMILGSVCTRACRFCNVKTGRPDLLDPHEPRRLAEAVQKLNLNHVVITSVDRDDLEDGGASHFAECINEIRRSSPNTTIEILTPDFLRKAGAVEVIANSKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEINEVVQVMDDLREANVDFLTIGQYLQPTKSHAEVIKYVTPEEFKYLERIAKTKGFLMVSATPLTRSSYHADKDFQKLKENYNIRLASM

Gene
lipA
Protein
Lipoyl synthase
Organism
Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas)
Length
297 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.676 kDa
Sequence
MRSKPDWLKVKMPTGDTFYQVRNLMKLYKLNTVCEEAACPNIGECWNKRHATVMILGSTCTRACAFCNVVSGIPDKLDPHEPQNLAKAVGLLKLEHVVITSVDRDDLEDGGSGHFVECIEEIRKNDQNVTIEVLTPDFLNKHGAIEKVADAAPDVYNHNIETVPRLYAKIRPKARYFHSLYLLKTVKYKNPKVFTKSGIMVGLGETKEEIYQVMNDLRSADVDFITIGQYLQPTPKHAAVDRYVTPEEFDHYKYVAYSKGFLMVASGPLVRSSYHAGEDFQRLKKNRAAMFMHAKSN

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Length
297 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.532 kDa
Sequence
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSDRVRARAKYERSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAGS

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia africae (strain ESF-5)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.514 kDa
Sequence
MANLNKRPDWIKVKAPNSTEYYNTKDLIKNLRLNTVCEEAACPNIGECWSKKHTTVMILGSVCTRACRFCNVKTGRPDLLDPYEPQRLAEAVQKLNLKHVVITSVDRDDLEDGGASHFAECISEIRKSSPNTTIEILTPDFLRKEGAAEIIANAKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEINEVVQVIDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERVAKTKGFLMVSASPLTRSSYHADEDFQKLKENYQQKLMS

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia canadensis (strain McKiel)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.516 kDa
Sequence
MANLNKRPDWIKVKAPNSVEYYNTKDLIKNLRLNTVCEEAACPNIGECWSKKHATMMILGSVCTRACRFCNVKTGRPDLLDPHEPQRLAEAVQKLNLKHVVITSVDRDDLEDGGALHFAECINEIRKSSPNTTVEILTPDFLRKEGAAEIIAHSKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHSIKKLSSEIFTKSGMMVGLGEKISEVIQVMDDLREAKVDFLTIGQYLQPTKDHAEVAKYVTPEEFKYLERVARTKGFLMVSASPLTRSSYHADEDFQKLKQNYRQSLVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.482 kDa
Sequence
MANLNKRPDWIKVKAPNSTEYYNTKDLIKNLRLNTVCEEAACPNIGECWSKKHTTVMILGSVCTRACRFCNVKTGRPDLLDPYEPQRLAEAVQKLNLKHVVITSVDRDDLEDGGASHFAECISEIRKSSPNTTIEILTPDFLRKEGAAEIIANAKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEINEVVQVIDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERVAKTKGFLMVSASPLTRSSYHADEDFQKLKENYQQKLVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia massiliae (strain Mtu5)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.46 kDa
Sequence
MANLNKRPDWIKVKAPNSTEYYNTKDLIKNLRLNTVCEEAACPNIGECWSKKHTTVMILGSVCTRACRFCNVKTGRPDLLDPHEPQRLAEAVQKLNLKHVVITSVDRDDLEDGGASHFAECISEIRKSSPNTTIEILTPDFLRKEGAAEIIANAKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPDIFTKSGMMVGLGEEINEVVQVMDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERVAKTKGFLMVSASPLTRSSYHADEDFQKLKENYQQKLVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia peacockii (strain Rustic)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.509 kDa
Sequence
MANLNKRPDWIKVKAPNSTEYYNTKDLIKNLRLNTVCEEAACPNIGECWSKKHTTVMILGSVCTRACRFCNVKTGRPDLLDPYEPQRLAEAVQKLNLKHVVITSVDRDDLEDGGASHFAECISEIRKSSPNTTIEILTPDFLRKEGAAEIIANAKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEINEVVQVIDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERVAKTKGFLMVSANPLTRSSYHADEDFQKLKENYQQKLVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.738 kDa
Sequence
MVTSPSGTGTRRMPPWLHKRLPASGDIEATRRLLADLHLNTVCQSARCPNQGECFASRTATFMILGNTCTRNCRFCAVEHGQPEAIDEDEPRRVAEAARRLGLKHVVVTSVTRDDLPDGGAGHFAATITALRQALPGAYIEVLTPDFRGSRAALAAVARARPDIFNHNVETVPRLYPDVRPQADYRRSLDVLKQMKELDATIYTKSGLMVGVGESREEVLAVMADLRAVNCDILTIGQYLRPSPRHLEIKEYVPPETFTWYAQKGREMGFLYVAAGPYVRSSYHAAEFSVKIAGVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.465 kDa
Sequence
MISGVDPQTHLPSGKPRWLKVKAPTSPGYLKLKGMLRQGGLHTVCEEATCPNIGQCWHEGSAAFMILGDTCTRRCAFCNVKTGKPLPPNPDEPQQLALTAQRMELKHVVITSVDRDDLEDGGAGQFIACIQALRRVLPEASVEVLTPDFRHKQGALERLVAARPDVFNHNVETVPRLYANVRPVSSYAFSLEVLRRAKQLNPEGMTKSGIMLGLGEDEAEVLAVFADLRAAGVDYLTVGQYLRPSPAHHAVVRYWEPERFEALGQQALQLGFKRVSSAPLARSSFHASELHGVDNA

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.008 kDa
Sequence
MPDPTSPKPDWLKVRLPRTDKYGAVKDVIKKYNLNTVCSSAMCPNAFECWDGGCLTFMVLGNTCTRACRFCTVTHGPAGEPLDSNEPQRLAAAAKELDLSYVVITSVDRDDLPDYGAGHYAACIRAVKEQLPGARVEAIIPDFTGRLDLLEQVVDARPDVISHNIETVERLSPSVRDRRAGYYRSLDVLRDVKRVNPHMLTKSSLLLGMGEEDIEIKEALHDLQEARVDIVTLGQYLRPSIRQWPVHRYVAPGEFSELAEYGRSLGFKYVAAGPFVRTSYRAGEQYVSVIADSRMA

Gene
lipA
Protein
Lipoyl synthase
Organism
Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.465 kDa
Sequence
MISGVDPQTHLPSGKPRWLKVKAPTSPGYLKLKGMLRQGGLHTVCEEATCPNIGQCWHEGSAAFMILGDTCTRRCAFCNVKTGKPLPPNPDEPQQLALTAQRMELKHVVITSVDRDDLEDGGAGQFIACIQALRRVLPEASVEVLTPDFRHKQGALERLVAARPDVFNHNVETVPRLYANVRPVSSYAFSLEVLRRAKQLNPEGMTKSGIMLGLGEDEAEVLAVFADLRAAGVDYLTVGQYLRPSPAHHAVVRYWEPERFEALGQQALQLGFKRVSSAPLARSSFHASELHGVDNA

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.008 kDa
Sequence
MPDPTSPKPDWLKVRLPRTDKYGAVKDVIKKYNLNTVCSSAMCPNAFECWDGGCLTFMVLGNTCTRACRFCTVTHGPAGEPLDSNEPQRLAAAAKELDLSYVVITSVDRDDLPDYGAGHYAACIRAVKEQLPGARVEAIIPDFTGRLDLLEQVVDARPDVISHNIETVERLSPSVRDRRAGYYRSLDVLRDVKRVNPHMLTKSSLLLGMGEEDIEIKEALHDLQEARVDIVTLGQYLRPSIRQWPVHRYVAPGEFSELAEYGRSLGFKYVAAGPFVRTSYRAGEQYVSVIADSRMA

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia rickettsii (strain Iowa)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.496 kDa
Sequence
MANLNKRPDWIKVKAPNSTEYYNTKDLIKNLRLNTVCEEAACPNIGECWSKKHTTVMILGSVCTRACRFCNVKTGRPDLLDPYEPQRLAEAVQKLNLKHVVITSVDRDDLEDGGASHFAECISEIRKSSPNTTIEILTPDFLRKEGAAEIIANAKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEINEVVQVIDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERLAKTKGFLMVSASPLTRSSYHADEDFQKLKENYQQKLVS

Gene
lipA
Protein
Lipoyl synthase
Organism
Rickettsia rickettsii (strain Sheila Smith)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.496 kDa
Sequence
MANLNKRPDWIKVKAPNSTEYYNTKDLIKNLRLNTVCEEAACPNIGECWSKKHTTVMILGSVCTRACRFCNVKTGRPDLLDPYEPQRLAEAVQKLNLKHVVITSVDRDDLEDGGASHFAECISEIRKSSPNTTIEILTPDFLRKEGAAEIIANAKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEINEVVQVIDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERLAKTKGFLMVSASPLTRSSYHADEDFQKLKENYQQKLVS

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.853 kDa
Sequence
MSALPAWLRVEARSYSEMAKVRSVLSRLGVYTVCEGARCPNVFRCWGEGTATFMILGEVCTRACRFCSVRTGNPRGYVDLDEPRRVAEAVRRLGLRYVVVTSVDRDDLPDGGAFQYASAIREIRRLAPGALVEVLTPDFRGSREAVETVAEAGPDVFAHNVETVRRLTPLVRDRRASYETSLRVLKTAKEVGCRLTKSGIMLGLGESFDEVVEVLDDLRKAEVDIVTIGQYVRPTKSARHLPVARWVPLEEFQKLGEVALSMGFKAVASAPLVRSSYRAEDLYEMALGLRPRAVLV

Gene
lipA
Protein
Lipoyl synthase
Organism
Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama)
Length
296 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.995 kDa
Sequence
MERTIEKPRIRVSADNRAFLETSRLVSACGLNTVCQEAACPNISECWSSKHVTVMILGSVCTRACRFCNVTTGKPELLDPHEPEKLASAVGKLGLRHVVITSVDRDDLDDGGAEHFASCVRRIRETSPGTSIEVLTPDFLGKVGARDIIIAAAPDVFNHNVETVPRLHPKIRIKARYFNSLSLLEEVKRKDPRIFTKSGLMLGLGEERSEVLQVMDDMRVAGIDFLTIGQYLRPSKKHMEVQRYATDEEFQYYKEAAYARGFLMVASSALTRSSYHADEDFLHLKNARAGALAKLV

Gene
lipA
Protein
Lipoyl synthase
Organism
Anaplasma phagocytophilum (strain HZ)
Length
295 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.254 kDa
Sequence
MNSKPSWLRVKMPGGEVFEEVRDLVKRQRLNTVCEEAACPNIGECWNKRHATIMVMGDVCTRACAFCNVKTGVPRALDLGEPERVGEAISKLGLKHVVITSVDRDDLPDGGASHFAKCIREIRKRDPNVTIEILTPDFQGKPGAVDVIASARPDVYNHNLETVPRLYARVRPRAKYFNSLQLLQQVKDKTQGVFTKSGLMLGLGEQKEEVYQVMDDLRCAGVDFLVLGQYLQPTKDNIDVDRYVTPEEFEQYKRMAYAKGFSMVASSPLARSSYHAEDDFLRLRALRTARMRVAT

Gene
lipA
Protein
Lipoyl synthase
Organism
Anaplasma marginale (strain St. Maries)
Length
295 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.168 kDa
Sequence
MENKPDWLRVRMPGGAVFDEVTELVRRYELNTVCEEAACPNIGECWNKRHATIMIMGSVCTRACAFCNVKVGVPNALDPDEPERVGAAISKLGLKHVVITSVDRDDLPDGGASHFAKCVREIRKRDSSVTVEILTPDFLGKPCAIDIIASARPDVYNHNLETVPRLYSRVRPRAKYFNSLNLLKEVKDKSPGVFTKSGFMLGLGESKEEVYQVMDDLRCAGVDFIVMGQYLQPTKNNIEVHRYVPPSEFEQYKLMAYAKGFSMVAASPLARSSYHAEDDFRKLKELRFARAKVNE

Gene
lipA
Protein
Lipoyl synthase
Organism
Baumannia cicadellinicola subsp. Homalodisca coagulata
Length
294 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.591 kDa
Sequence
MVKIEKKLHKPLWLKIKLPSSDYKIKVIKKTMNKSSLYTICEEACCPNLAECFNNGTATFMILGNICTRRCPFCNVAHGRPLIPDIHEPEKLAETITNMGLRYVVITSVNRDDLYDGGAQHFVDCIRAIRAKNSATRIEVLVPDFRGHMKTALEILNTSPPDVFNHNIENVPRLYRHIRPGADYHRSLKLLKKFKEYNPSLPTKSGLMMGLGETREEIIEVMRDLRQHNVTMLTLGQYLQPSSNHLPVQRYITPQEFNEMKLESLAMGFTYAACGPFVRSSYHADLQNKGIEVK

Gene
lipA
Protein
Lipoyl synthase
Organism
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
Length
294 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.636 kDa
Sequence
MEHVPGKKPEWLKIRLSSGASFASTKRLLDRHSLHTVCRSAMCPNLQECWSRGTATFLLLGTVCTRNCRFCAVGKASNPPAPDPREPEKIALAVHSMQLKHTVLTSVTRDDLPDGGAEYWVATIRAIRTLNPFVTIECLIPDFEGNERAMDLVMAELPEILNHNIETVPSLYTKVRPQANYATSLRLLQRAKEMHGLTTKSGMMVGMGETAEEVAISLGDLLLHGCDMVTIGQYLQPSALHLPVERYITPEEFEQYRSFAEGAGFRHVQSGPFVRSSYHAEALTKKTETVCSPI

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacter daltonii (strain DSM 22248 / JCM 15807 / FRC-32)
Length
294 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.559 kDa
Sequence
MKITRRPEWLQKKVSPAAHADMERLLGGLQLHTVCQEAHCPNISECFRQRQATFLILGKLCTRLCSFCNVTKQTPLAVDQAEPERVAAAVELLKLTHVVVTSPTRDDLADGGAALYAATVAAIRNASPQTKIELLVPDFAGNQESIAAVVSACPHILGHNLETVPRLYSIRSGADYRRSLLMLEMIRRLNPAMKTKTGLMLGLGETEEELFQALRDLRRVDCSYLSLGQYLAPSRSHYPVQDYPSPETFDRYREQALSMGFEHVESGPYVRSSYHAEHYGTGTGHAKLSPAPAD

Gene
lipA
Protein
Lipoyl synthase
Organism
Anaeromyxobacter dehalogenans (strain 2CP-C)
Length
294 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.217 kDa
Sequence
MDAKKPSWLRVNVPGGERYQKVRETLKGLQLHTVCAEAHCPNVAECWGGGTATVMLMGDVCTRGCRFCNVKTAAHPPALDPDEPRHLAAAIAELGLDYIVVTSVDRDDLPDGGAAHFADAIRRLKEIPGLLVEVLTPDFRGDPAAVRTVGRAAPDVFANNLETVRRLTPAVRDAKATYDQTLGVLAQMKREFPQVVTKSSIMVGLGEQEAEVVEAMRDLRANGVEILTLGQYLRPSAWHLPVVEYVSPERFAAYRDQGLALGFRYVASGPLVRSSYRAAELFLRGEIESRTKPR

Gene
lipA
Protein
Lipoyl synthase
Organism
Anaeromyxobacter sp. (strain Fw109-5)
Length
294 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.204 kDa
Sequence
MTARKPGWLRVNVPGGARYQQVRDTVKGLALHTVCEEAHCPNVAECWGGGTATVMLMGDVCTRGCRFCNVKTDAHPPPLDPDEPRHLAEAIAELGLDYIVVTSVDRDDLPDGGAGHFADAIRRLKDIPQLLVEVLTPDFRGDAEAVRTVGRARPDVFANNLETVRRLTPVVRDLKAGYDQTLAVLARMKREFPRIVTKSSIMVGLGETEDELLEAMGDLRAAGVEILTLGQYLRPSAWHLPVVEYVKPEKFAAWREAGLGLGFRYVASGPLVRSSYRAAELFLRGELASRPPGP

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlorobium chlorochromatii (strain CaD3)
Length
293 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.183 kDa
Sequence
MAQPIGRKPEWLKIKMASGASFAATRQLLNRHSLHTVCRSALCPNLQECWSRGTATFLLLGNTCTRSCTFCAVSKASAPPAPDSDEPQKIAEAIASMKLKHAVLTSVTRDDLPDGGANHWIATMQAIRQRTPNVSLECLIPDFQHKKAALDSVMQATPDVLNHNIESVPSLYSTVRPQANYRASLELLRYAKEQHGLATKSGLMVGMGEERHEVEATLHDLAAHGCDMVTIGQYLQPSAAHLPVARYVPPQEFEEYSTIAKNAGIRYVHAAPFVRSSYHAETFPNNLTITQNL

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Length
293 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.233 kDa
Sequence
MEAAKPRLRVRINDSYVKVARLVAGLGVATVCEGALCPNIFTCWGEGTATFMIMGDTCTRGCRFCYVKKGVPEPLDPLEPYKVALAVDALGLDYVTLTSVDRDDLPDGGASHFAATVRAIKRLRPDTIVEALIPDFQGVEEHVRLVAASGLEVLAHNIETVERLTPLVRDRRAGYRQSLRVLEIAKEEGVVTKSSILLGLGEDKSEVIEAMRDLRSVGVDILVLSQYYRPSRKQLPVAKRYSLSEFRELAEKGLRMGFAYVVAHPLARTSFKAKEAYLAAVRRVEAEGGGRRA

Gene
lipA
Protein
Lipoyl synthase
Organism
Gramella forsetii (strain KT0803)
Length
293 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.33 kDa
Sequence
MNTDVAPVKSKTERKPKPKWLRVKLPTGKKYTELRNLVDKYDLHTICTSGSCPNMGECWSEGTATFMILGNVCTRSCGFCGVKTGRPETVDWDEPEKVARSIKLMQIKHAVVTSVDRDDLKDMGSIVWAETVKAIRRMNPETTLETLIPDFQGNERNIDRIIEVAPEVVSHNMETVKRLTREVRIQAKYDRSLAVLKYLKDNGIRRTKSGIMLGLGEQEEEVIQTLKDLREAGVDVVTIGQYLQPSKKHLPVKQFITPDQFQKYEKIGLELGFRHVESSALVRSSYKAQKHLN

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
Length
292 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.542 kDa
Sequence
MNRERQKKPEWLKLKLSTGEHFAATRQLLSGLRLNTVCRSAMCPNLQECWSKGTATFMLLGSVCTRTCRFCAVDKTVLPVPPDPEEPEKIALAVKSMSLKHVVLTSVNRDDLPDGGSGHWVSSIRSIRSLNPEVSIECLVPDFDGITANADRVMQEAPEVLNHNIETVPSLYPAVRPQADYRRSLELIERAKAVFRLSTKSGMMVGMGETGDEVAASLGDLRASRCDIVTIGQYLQPTAAHLPVNRYVTPDEFEEYKNRAESLGFRHVQSGPFVRSSYHAEEFVAARHIERC

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlorobaculum parvum (strain NCIB 8327)
Length
292 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.438 kDa
Sequence
MNSGPGKKPDWLKIKLTSGSSFASTKKLLNKHSLHTVCRSAMCPNLHECWSKGTATFLLLGNVCTRSCRFCAVGTERRPAMPDPEETAKIGEAVKAMKLRHAVLTSVNRDDLADGGAAHWVETIRAIREVNPGVSIECLIPDFQGDEQALDSVMRERPEVLNHNIETVPSRYASVRPQASYERSLAVIERAKRQFRLATKSGMMVGMGETPEEVNAALRDLRAHGCDMVTIGQYLQPTATHLPVSRYVTPEEFERYREIALDAGFRHVQSGPFVRSSYHAEAFEPVEEISNS

Gene
lipA
Protein
Lipoyl synthase
Organism
Ehrlichia ruminantium (strain Gardel)
Length
292 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.219 kDa
Sequence
MKSKPDWLKVKMPTGSAFYEMRNLMKLHKLNTVCEEAACPNIGECWNKKHATVMILGSTCTRACAFCNVASGIPDKLDPHEPQSLAKAVSSLKLQHVVITSVDRDDLEDGGAGHFVECIEEIRKRDSNVTIEILTPDFLNKHDAIDKIAKAFPDVYNHNVETVPRLYAKIRPKARYFHSLYLLKTIKQKNPRIFTKSGIMVGLGELKEEIYQVMDDLRSADVDFIVIGQYLQPTSKHAVVDRYVTPEEFDHYKYVAYSKGFLMVASGPLVRSSYHAEEDFQRLKKNRAAMYT

Gene
lipA
Protein
Lipoyl synthase
Organism
Ehrlichia ruminantium (strain Welgevonden)
Length
292 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
33.219 kDa
Sequence
MKSKPDWLKVKMPTGSAFYEMRNLMKLHKLNTVCEEAACPNIGECWNKKHATVMILGSTCTRACAFCNVASGIPDKLDPHEPQSLAKAVSSLKLQHVVITSVDRDDLEDGGAGHFVECIEEIRKRDSNVTIEILTPDFLNKHDAIDKIAKAFPDVYNHNVETVPRLYAKIRPKARYFHSLYLLKTIKQKNPRIFTKSGIMVGLGELKEEIYQVMDDLRSADVDFIVIGQYLQPTSKHAVVDRYVTPEEFDHYKYVAYSKGFLMVASGPLVRSSYHAEEDFQRLKKNRAAMYT

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlorobium luteolum (strain DSM 273 / 2530)
Length
291 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.861 kDa
Sequence
MKDHSPRKPEWLKQRLSAGDGFGALQRLLSSKGIHTVCRSAKCPNLQECWSEGTATFLLLGNVCTRTCRFCAIDTSRTPAAPETDEPERVAAAARTMALQFVVLTSVTRDDLPDGGAAHWVETIRAIRKASPRAGIECLIPDFAGNEAALDLVCKERPDVLNHNIETVPRLYEKVRPEARYRRSLDLLQRAASLFGLTTKSGMMVGMGESFEEVGEALQDLARHGCRMITIGQYLQPSARHIPVERYVTPEEFAGFRDLALSLGFSSVQSGPFVRSSYHAAASSAACTPVP

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622)
Length
291 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.136 kDa
Sequence
MDPIRKPAWLQKKIIPAAHAEMEGLLKELRLNTVCQQARCPNITECFGKRQATFLILGRICTRLCSFCSVSKETPLPLEPGEAASVAEAVKRLGLSHVVITSPTRDDLPDGGASVYAETVARIRSVSPATKVELLIPDFRGDWAALAAVVESAPDILGHNLETVPRLYSIRSGADYRRSLDLLAQARRMAPGLNTKSGLMLGLGEEEAELFAVMEDLLKAGCGYLSLGQYLAPSRMHHPVQRYVEPELFERYKERALTMGFEHVESAPYVRSSYHAENYLESKFPPPEGEG

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacter sp. (strain M21)
Length
291 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.095 kDa
Sequence
MDPIRKPAWLQKKITPAAHAEMEGLLKELRLNTVCQQARCPNITECFGKRQATFLILGRICTRLCSFCSVSKETPLPLEPGEAASVAEAVKRLGLSHVVITSPTRDDLSDGGASVYAETVARIRSVSPRTKVELLIPDFRGERAALAAVVESAPDILGHNLETVPRLYSIRSGADYQRSLDLLAQARRMAPDLNTKSGLMLGLGEEEAELYAVMEDLLKAGCGYLSLGQYLAPSRMHHPVQRYVEPELFEKYKEKALAMGFEHVESAPYVRSSYHAENYLEVKSPPPEGEG

Gene
lipA
Protein
Lipoyl synthase
Organism
Desulfovibrio alaskensis (strain G20)
Length
291 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.016 kDa
Sequence
MSAQENSAPFLRIPPWLRTRIPCNRTYTATRELIGDLNLHTVCQSAKCPNMFECFSSRTATFLILGGTCTRNCAFCNIEPGDVLPPDAGEPQRVALAAARLELKHVVITSVTRDDLPDGGAAHFAATIQAVRSRLPRCTVEVLIPDFQGDAAALQTVLQARPDVLNHNVETPPAHYSRIRPQADYSQSLELLRRARAAGFTVKSGLMTGLGETDAEVLGVIDDLCATGCNIVTVGQYMRPSRRHPAVQRYVHPDMFEEYAAYGRARGIPHMFCAPLVRSSYNASMFVQEKN

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Pyrobaculum calidifontis (strain JCM 11548 / VA1)
Length
291 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.867 kDa
Sequence
MELPSWIRVKAGDYGRIVAVREAVFAAGVHTICEEAHCPNIFSCWGEGTATFLILGDVCTRACKFCAVKTGDPRGFVDPTEPARVAEAVAKLGLRYVVITSVDRDDLPDGGASQFASVVKAVKARAPWAKVEVLTPDFGGSAEAVASVVEAGPDVYAHNLETVRRLTPLVRDRRASYDVSLRVLKMAKELGAVTKSGLMVGLGETFDEVLEALSDLRRVDVDIVTIGQYLKPRGHKRFLEVQRWVPPEEFEKYREAAEAMGFKAVVAGPLVRSSYKAHEAYLEMLRKTIGR

Gene
lipA
Protein
Lipoyl synthase
Organism
Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
Length
291 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.828 kDa
Sequence
MSYLKKPDWLKIRVKADQKIDDVIEILKMFSLHTVCEEAQCPNIYECFSKKTATFLIMGDVCTRNCTFCDVKKGKPVKLNSDEPKMVANAVGALGLKYVVITSVTRDDLPDGGASHFAECIRSIKGKRPYTKIEVLIPDFKGSFESVSKVVEASPDVVAHNIETIERLYPCVRPLASYKRSLDVLRMVKEIDKNIFTKSGIMVGLGETKDEVKKALEDLRNAECDFVTIGQYLSPSKNHHPVVEFVHPDVFEEYKEFAISIGFKFVMSGPLVRSSYMAENTKDIIENVRKI

Gene
lipA
Protein
Lipoyl synthase
Organism
Wolbachia pipientis subsp. Culex pipiens (strain wPip)
Length
290 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.679 kDa
Sequence
MHSKPTWLRAKAPAGKVFNETLNTVKLHNLHTVCEEAACPNIGECWNKRHATVMILGSVCTRACAFCNVATGIPDKLDPHEPENLAKAIKKLNLKHVVITSVDRDDLSDGGANQFIRCIEEIRKITSETTIEILTPDFLNKKGAFEAIAIASPDVYNHNIETVPRLYAKIRPRARYFHSLYLLKMVKQINPKLFTKSGLMVGLGETKEEIFQVMDDLRSAEVDFITIGQYLQPTPKHAKIDRYVTPEEFEHYKYIAYSKGFLVVASSPLTRSSYHAEEDFNRLAAAKTST

Gene
lipA
Protein
Lipoyl synthase
Organism
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
Length
290 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.688 kDa
Sequence
MIELPVVPSASDRKSKPDWLRVKLPIGKEYTKLRALVDEHKLHTICQSGNCPNMGECWGAGTATFMILGNVCTRSCSFCAVATGRPTEYDIDEPKRVAEAVRLMNVKHCVITSVNRDELKDKGAEVWYQTVVRVKEESPQTTIETLIPDVKSDWASLERMISGGQEVVSHNMETVERLYRRVRPQAKYSRSLEEIQRIKAFGKRTKSGIMLGLGETKDEVLKAMDDLVAHGLDVLTLGQYLQPTKMHLEVAEFIHPDQFAEYKEIGLSKGLNYVESGPLVRSSYHAEKHI

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Length
290 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.248 kDa
Sequence
MNSGPGKKPDWLKIKLASGSSFASTRKLLNRHSLHTVCRSAMCPNLHECWSKGTATFLLLGNVCTRSCRFCAVGTECRPAMPDPEEPSKIAEAVKTMKLRHAVLTSVNRDDLADGGATHWVETIRAIREVNPGVSLECLIPDFSGNEQSLDLVMQELPEVLNHNIETVPSRYAAVRPQALYERSLAVIERAKRQFRLATKSGMMVGMGETEEELEASLHDLRGHGCDMVTIGQYLQPTAAHLPVSRYVTPEEFERYREIALDAGFRHVQSGPFVRSSYHAEAFEPVEKIS

Gene
lipA
Protein
Lipoyl synthase
Organism
Flavobacterium psychrophilum (strain JIP02/86 / ATCC 49511)
Length
290 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.926 kDa
Sequence
METVLDSNILPVGKPKWLKVKLPIGQKYTELRGLVDKYKLNTICTSGSCPNMGECWGEGTATFMILGNICTRSCGFCGVKTGRPETVDWDEPEKVARSIKIMNIKHAVITSVDRDDLKDMGSIIWIETVKAIRRMNPETTLETLIPDFQGVERNLDRIVAANPEVVSHNVETVRRLTREVRIQAKYDKSLEVLRYLKAKGIKRTKSGIMLGLGETEEEVIQTMRDLREANVDIVTIGQYLQPSKKHLPVKEFITPEQFEKYELLGKEMGFRHVESGPLVRSSYHAQKHIL

Gene
lipA
Protein
Lipoyl synthase
Organism
Alkaliphilus metalliredigens (strain QYMF)
Length
290 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.42 kDa
Sequence
MNIKRKPEWLRIKLGEGRNLNYVKGLLKKFSLNTVCEEANCPNQIECFSKKTATFMILGSDCSRSCGFCNVSHGALQPIDPNEPENVANAVAELGLKHVVITSVTRDDLADGGAQHFADVVNQIKSKNKETMIEVLIPDFQGNKEALQKVVQSKPDIINHNMETIPRLYPEIRPKAEYVQSLELLKNVKEMDPEILTKSGVMVGLGEGEEELIEVFKDLRGSGCDFLTVGQYLPPSTKHYPLKAYISPEVFERYKEEALKIGFSFVASSPLVRSSYNAAEALEKHEEMKS

Gene
lipA
Protein
Lipoyl synthase
Organism
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Length
290 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.592 kDa
Sequence
MNFKAGFMTCNQRKPDWLKIKLPTGELSQEVSNTIKIHKLNTICTSGKCPNQGECWRCGTATFMICGNICTRACKFCNVPTGCPLPLNPNEPMEIAQSVEALKLKHVVLTSVDRDDIKDFGASHWVKVIRAVKQKTPNVTMEVLIPDFQGHEDLVSMIIEAKPEVISHNLETVRRLSPHVRSRATYDTSLKVLKQIADSGLVCKSGIMLGLGETRAEILETMDDLRKINCKVMTIGQYLRPSIKNIEVKEYVRPEVFEEYKQIGLEKGFSFVESGPLVRSSYHAEKHVLS

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Length
290 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.806 kDa
Sequence
MIPSWVSLRAGDYEKIINVRRALSRHGIYTVCEGAKCPNIFHCWGEGTATFMILGEVCTRACRFCAVRTGNPRGYVDWGEVDRLVEAVRELGLKYVVVTSVARDDLPDGGASVFAAVVKKLREVGCVVEVLVPDFGGSPASVKTVVSSGPDVFAHNVETVRRLTPLVRDRRAGYERSLSVLKYAKEFGAPLTKSGLMLGLGETFEEVVETLEDLRRADVDIVTIGQYIKPSGSPRHLNPVRYATPEEFAKIKEVAVSLGFKAVASGPLVRSSYKAYSLYREALKNIVYLG

Gene
lipA
Protein
Lipoyl synthase
Organism
Synechococcus sp. (strain RCC307)
Length
289 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.139 kDa
Sequence
MQKPEWLRVKAPQRERIGAVADLLLDLKLNTVCQEASCPNIGECFAGGTATFLIMGPGCTRACPYCDIDFDKSVRELDPTEPERLGEATQRLGLKHVVITSVNRDDLADGGASQFVACIEQIRRRSPGTTIELLVPDFCGDWDALAAVMAGAPDVLNHNIETVPRLYKKARPQAIYERSLELLQRVRQGWPRCYSKSGLMVGLGETDAEVIEVLADLRRHAVDIVTIGQYLSPGPKHLPVDRFVSPEQFEQFRSQGESELGFLQVVSTPLTRSSYHAGEVQRLMQEHPR

Gene
lipA
Protein
Lipoyl synthase
Organism
Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101)
Length
288 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.816 kDa
Sequence
METVIENIPPAKPKWLKVKLPIGQKYTELRGLVDKYSLNTICTSGSCPNMGECWGEGTATFMILGNVCTRSCGFCGVKTGRPETVDWDEPEKVARSIKIMNIKHAVITSVDRDDLKDGGSIIWMETVRAIRRMNPNTTLETLIPDFQGIERNIDRIVEANPEVVSHNMETVRRLTREVRIQAKYDRSLEVLRYLKEKGINRTKSGIMLGLGETEEEVYQTMRDLRDANVDVVTIGQYLQPTKKHLPVKEFITPELFAKYEKYGIELGFRHVESGPLVRSSYKAQKHIL

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
Length
288 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.108 kDa
Sequence
MGNDKRVRKPEWLKISIGANERYTETKRIVESHCLHTICSSGRCPNMGECWGKGTATFMIAGDICTRSCKFCNTQTGRPLPLDPDEPTHVAESIALMKLSHAVITSVDRDDLPDLGAAHWAQTIREIKRLNPETTTEVLIPDFQGRKELVDQVIKACPEIISHNMETVKRISPQVRSAANYHTSLEVIRQIAESGITAKSGIMVGLGETPAEVEELMDDLISVGCKILTIGQYLQPTHKHFPVAAYITPEQFAVYKETGLKKGFEQVESAPLVRSSYHAEKHIRFNNK

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacteroides fragilis (strain YCH46)
Length
288 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.092 kDa
Sequence
MGNDKRVRKPEWLKISIGANERYTETKRIVESHCLHTICSSGRCPNMGECWGKGTATFMIAGDICTRSCKFCNTQTGRPLPLDPDEPAHVAESIALMKLSHAVITSVDRDDLPDLGAAHWAQTIREIKRLNPETTTEVLIPDFQGRKELIDQVIKACPEIISHNMETVKRISPQVRSAANYHTSLEVIRQIAESGITAKSGIMVGLGETPAEVEELMDDLISVGCKILTIGQYLQPTHKHFPVAAYITPEQFAVYKETGLKKGFEQVESAPLVRSSYHAEKHIRFNNK

Gene
lipA
Protein
Lipoyl synthase
Organism
Wolbachia pipientis wMel
Length
287 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.496 kDa
Sequence
MHSKPQWLRAKAPTGEVFNETLNIVKLHNLHTVCEEAACPNIGECWNKRHATVMILGSVCTRACAFCNVATGIPDKLDPHEPENLAKAIKKLNLKHVVITSVDRDDLPDGGANQFIQCIEEIRKITSETTIEILTPDFLNKKGAFEAIAVASPDVYNHNIETVPRLYAKIRPRARYFHSLYLLKMVKQINPKVFTKSGLMVGLGETKEEILQVMDDLRSAEVDFITIGQYLQPTPKHAKLDRYVTPEEFEHYKYIAYSKGFLVVASSPLTRSSYHAEEDFNRLKACR

Gene
lipA
Protein
Lipoyl synthase
Organism
Wolbachia sp. subsp. Brugia malayi (strain TRS)
Length
287 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.429 kDa
Sequence
MHSKPPWLRAKAPTGEIFNETLNTVKLHGLHTVCEEAACPNIGECWNKRHATVMILGSVCTRACAFCNVATGIPNKLDPHEPENLAKAIKKLNLKYVVITSVDRDDLPDGGASQFIKCIEEIRKITPETTVEILTPDFLNKKGAFEAIAVASPDVYNHNIEMVPRLYARIRPRARYFHSLYLLKMVKQINPKLLTKSGLMVGLGETKEEVLQVMDDLRSAEVDFITIGQYLQPTPKHAKIDRYVTPEEFEHYKYIAYSKGFLVVASSPLTRSSYHAEEDFNRLKACR

Gene
lipA
Protein
Lipoyl synthase
Organism
Wolbachia sp. subsp. Drosophila simulans (strain wRi)
Length
287 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.531 kDa
Sequence
MHSKPQWLRAKAPTGEVFNETLNIVKLHNLHTVCEEAACPNIGECWNKRHATVMILGSVCTRACAFCNVATGIPDKLDPHEPENLAKAIKKLNLKHVVITSVDRDDLPDGGANQFIQCIEEIRKITSETTIEILTPDFLNKKGAFEAIAVASPDVYNHNIETVPRLYAKIRPRARYFHSLYLLKMVKQINPKVFTKSGLMVGLGETKEEIFQVMDDLRSAEVDFITIGQYLQPTPKHAKLDRYVTPEEFEHYKYIAYSKGFLVVASSPLTRSSYHAEEDFNRLKACR

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlorobium phaeobacteroides (strain DSM 266)
Length
287 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.109 kDa
Sequence
MSNVLARKPDWLKLRLSAHGEFAATRQLLEQRNLNTVCRSAMCPNLQECWSRGTATFLLLGNICTRTCRFCAVGTASIPPMPDSLEPENIAEAVEIMNLNHVVLTSVNRDDLADGGARHWQKTMQAVRQRNPKVTLECLIPDFQAQTEALDIVLAEAPEVLNHNIETVPSIYHIVRPEANYSSSLNIIRRAKEHFNLTTKSGLMVGMGETFDEVVQSLHDLVQHGCDMVTIGQYLQPSASHIPVNRYVTPEEFDRYKTVAESLGLRNVRSGPFVRSSYLAETLSPDH

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
Length
286 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.253 kDa
Sequence
MNAGPINYKVKLPSGERYTFIKSTLSARNLYTVCEEAHCPNIAECWESGTATFMIMGSNCSRGCRFCAVTHGRMLPLDPMEPEKVYESVKMMNLDYVVITSVDRDDLPDKGSSHFAAVIRRLKDLKIKIEVLIPDFSGVHKFIDKIIDERPDVIAHNIETVRRLTKTVRDPRAGYDQSLNVLRYVKSRSNIITKSSIMLGLGETDDEVIETLHDLHDAGVDIVTIGQYLRPTKKQLEVKEYSPMERFKNLEESAYSIGFSFVASGPLVRTSYRAAEAFVKGGFKND

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Length
286 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.142 kDa
Sequence
MKSEVVVRINENFKKLSRIVSEKGISTVCEEALCPNIMECWGSGTATFMIMGDICTRGCRFCYVKKGKPVLLDHEEPIKVAEAVREMGLDYVVITSVDRDDLADGGASHFSQVVKAVKEMNPDVIVEVLTPDFMGNKELVEKVIGSGVDVFAHNVETVRSLTPLVRDARASYEQSLRVLSYAKNVVKKSSILLGLGESLEEVVETMKDLRNVGVDILVLSQYMRPSIKQLEVKKRYNMEEYKELEKIAYSLGFSYVVALPHARTSYRAKEAYLRAMANVKNNNRWS

Gene
lipA
Protein
Lipoyl synthase
Organism
Sulcia muelleri (strain GWSS)
Length
286 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.985 kDa
Sequence
MKKNKNINFKPKWLRVKSPDKYNNIYKISNYNNLNTICKSGSCPNIAECWEQGVATFMILGNICTRSCKFCGVKTGKPNKIDFYEPKKIAHNIKIMKIKHAVITSVDRDDLKDMGAIIWGKTIKAIKNINEKISLETLIPDFKGRKDLINIIVNEKPEVISHNIETVRRLTKKVRTQAKYDRSINVLKYIKLISNIRTKTGIMLGLGETEEEVIQTLKDSRNANIDIITIGQYLSPSIKHFYVKKFIPPYIFKKYENIALDMGFLYVESGPLVRSSYNAYKHIFLK

Gene
lipA
Protein
Lipoyl synthase
Organism
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T 6331)
Length
285 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.331 kDa
Sequence
MMQTKKPDWLRIRIKANQSVEEVIKLLKDLSLHTVCQEAQCPNIFECFSKKTATFLILGDVCTRNCTFCDVKKGKPQEVDKNEPKKIAEAVKVLNLSYVVVTSVTRDDLEDGGAEHFANVIEKIKELNPQTKVEVLIPDFNGDEKAIYKVVSARPDVLSHNVETVPRLYPTVRSKADYERSLSVLKVAKKMDNRIYTKSGLMVGLGETKEEVKEVLKNLRSVGCDFVTIGQYLSPSKQHYPVIEYIHPNVFEEYKEYAISIGFKHVMSAPLVRSSYLAEETTKII

Gene
lipA
Protein
Probable lipoyl synthase
Organism
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Length
285 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.111 kDa
Sequence
MEKKVQIAVYENENFKRVAEIVKKKSIATVCEEALCPNIMECWGSGTATFMIMGSICTRGCRFCYVLKGKPSPLDDEEPKRVAEAVKEMELDYVVITSVDRDDLSDGGAQHFANVVKTVKELNPGIIVEVLTPDFRGNIDAVKKVIDAGVDVFAHNVETVRRLTPIVRDPRASYEQSLNVLKYAENVIKKSSILLGLGETWDEIVETMRDLRSVGVSILVLSQYMRPSRKQLEVKKRYTLEEFKELEEIAYSMGFSAVISLPLARTSYKAKEAYFRAIENAKNHS

Gene
lipA
Protein
Lipoyl synthase
Organism
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
Length
284 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
32.154 kDa
Sequence
MTVRKPEWLKVRILSEDLNRMEAFLKNMALNTVCQSANCPNMGECFARRTATFMIMGNICTRNCRFCAVEKGHPQPLDEEEPRRVAEAARRLGLRHVVVTSVTRDDLPDGGASHFAKTIYELKKLPGVTVEVLVPDFMGNEEAIRTVVEAKPDVINHNVETVPRLYSRVRPKADYIRSLNLLKKVKELDPLILTKSGIMVGLGETEEEVIEVMKDLRDIDCDMMTIGQYLRPSHKHIEVAEYVTPEQFKRYEEIGYKLGFKHVASGPLVRSSYHADVGLSLARG

Gene
lipA
Protein
Lipoyl synthase
Organism
Chlorobium phaeovibrioides (strain DSM 265 / 1930)
Length
284 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.507 kDa
Sequence
MPGQRLRKPEWLKLRMRTGPEFGDIQRLLSETSLNTVCRSAMCPNLQECWSRGTATFLLLGNVCTRSCRFCAIGTQQKPIPPDPKEPARIAGAVTAMKLNFVVLTSVNRDDLPDGGARHWTETMKAIRLSSPDAGLECLIPDFEGNDEALDMVMNERPDVLNHNIETVPRLYTNVRPEASYNQSLSILDRALTLHGLATKSGMMVGMGETFEEVVASMKDLREAGCSRLTIGQYLQPTASHFPVERYVPPEEFDAYRDEALGMGFSTVQSGPFVRSSYLAGSEE

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / NBRC 14291 / NCTC 11154)
Length
284 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.725 kDa
Sequence
MNHVKKPDWLKINIGANARYTETKHIVDSHKLHTICSSGRCPNMGECWGKGTATFMIGGEICTRSCKFCNTQTGRPLPLDPEEPTHVAESIQLMKLSHAVITSVDRDDLDDLGAAHWAKTISEIKRLNPETTTEVLIPDFQGKSELIQLVIDAKPDIISHNMETVRRISPLVRSAANYATSLKVIKQIANNGITAKSGIMVGLGERPEEVEEVMDDLLAQGCKILTIGQYLQPTHRHYPVAEYITPDQFKQYRTIGLKKGFREVESAPLVRSSYHAEKHIKFKG

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
Length
283 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
30.825 kDa
Sequence
MTIVRKPQWLQKKINPAAHAGMEGLLGELRLHTVCQEARCPNITECFRERQATFLILGAACTRLCSFCNVTKQTPIPPDPGEPDRVAEAIRRLGLSHVVITSPTRDDLPDGGAGHYAETVAAIRSASPATTVELLIPDYLGNRESLARVVASAPAIIGHNVETVPRLYQIRAGADYGRSLGVLRTLRELDPVVRSKSGIMLGLGEAEEEVLAVFADLRSVGCSYLSIGQYLAPSKSHHPVREFIPPECFERYRAAALATGFAHVESGPYVRSSYHAARYDGQL

Gene
lipA
Protein
Lipoyl synthase
Organism
Desulfotomaculum reducens (strain MI-1)
Length
283 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.512 kDa
Sequence
MNKRKPDWLKIKLQGAEKSHEVKDMLKRLSLHTVCEEANCPNLIECFGRKTATFMILGSVCTRNCTFCNVTKGLTQAVDAEEPSNVAQAVKELGLKHVVITSVTRDDLPDGGAGHFAKVIEKLRPTEVIVEVLIPDFQGDREALDTVIRAKPHILNHNIETVPRLYATVRPKASYARSLELLKNSKELDPGIFTKSGIMVGLGEQEEEVIAVLQDLRAVDCDLLTIGQYLAPSAKHHPVIEYIHPELFKKYKDVAYEMGFKYVASDPLVRSSYHAADVSHIIG

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacter uraniireducens (strain Rf4)
Length
283 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.376 kDa
Sequence
MKITRRPEWLQKKISPSAHAEMERLLGDLQLHTVCQEAHCPNISECFRSRQATFLILGNICTRLCSFCNVTKQSPHHFDPDEPARVAAAVQKLQLSHVVITSPTRDDLPDGGAGLYAQTVTAIRKAAPQTAIELLIPDFMGDHGSIAAVVAACPDISGHNLETVPRLYHIRSGADYRRSLDVLKIIHDLDPRLLTKSGLMLGLGETEVEIFQVLDDLLAVGCSYLSLGQYLAPSRSHYPVQGYVPPEIFDNYRERALAMGFKHVESGPYVRSSYHAEQYGMKG

Gene
lipA
Protein
Lipoyl synthase
Organism
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Length
282 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.299 kDa
Sequence
MAQHVKKPEWLKIRLGGNEKFTETKSIVEGHCLHTICTSGKCPNMGECWSRGTATFMIGGDICTRACRFCNTLTGRPKPLNEAEPTHVALSIKLMGLNHAVVTSVDRDDLPDYGATHWVKTIQEIRRINSGVTLEVLIPDFKGRMDLVDMIIEASPDVISHNLETVRRLTPSVRSVATYDTSLAVLRHIAQSGKMPAKTGMMLGLGETEEEILELMDDALAAGVSVITIGQYLQPSRKNLPVVEYITPEQFEHLRLVGIEKGFRTIESAPLVRSSYHAERHL

Gene
lipA
Protein
Lipoyl synthase
Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Length
282 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.269 kDa
Sequence
MAQHVKKPEWLKIRLGGNEKFTETKSIVEGHCLHTICTSGKCPNMGECWSRGTATFMIGGDICTRACRFCNTLTGRPKPLNEAEPTHVALSIKLMGLNHAVVTSVDRDDLPDYGAAHWVKTIQEIRRINSGVTLEVLIPDFKGRMDLVDMIIEASPDVISHNLETVRRLTPSVRSVATYDTSLAVLRHIAQSGKMPAKTGMMLGLGETEEEILELMDDALAAGVSVITIGQYLQPSRKNLPVVEYITPEQFEHLRLVGIEKGFRTIESAPLVRSSYHAERHL

Gene
lipA
Protein
Lipoyl synthase
Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Length
282 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.352 kDa
Sequence
MADRVRKPEWLKINIGANDRYTETKRIVDSHCLHTICSSGRCPNMGECWGKGTATFMIGGDICTRSCKFCNTQTGRPHPLDANEPTHVAESIALMKLDHAVVTSVDRDDLPDLGAGHWAHTIREIKRLNPQTTIEVLIPDFQGRMELVDLVIEANPDIISHNMETVRRISPLVRSAANYDTSLQVIGHIARSGTKSKSGIMVGLGETPQEVETIMDDLLAVGCQILTIGQYLQPTHRHYPVAEYVTPQQFATYKTIGLEKGFSIVESAPLVRSSYHAEKHIR

Gene
lipA
Protein
Lipoyl synthase
Organism
Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ)
Length
281 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
30.643 kDa
Sequence
MKIQRKPEWLRKKVPQGEQAAMRGLLSELKLNTVCQQALCPNIAECFGCGQATFLILGRDCTRQCSFCNVDKAPRPQAPDADEPRRLAEAVLRLKLSHVVITSPTRDDLADGGAGHYAATVAAVREVSPGTAVELLVPDFGGDHAALATVLAAQPSILAHNLETVPRLYEVRKGADYQRSLDLLQQAALRAPAIPTKSGIMLGLGEELDEVRAVLQDLRRVGCSYLSLGQYLAPSKRHQPVVAYIPPQQFDLLRDEALALGFRHVESGPYVRSSYHAANYA

Gene
lipA
Protein
Lipoyl synthase
Organism
Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)
Length
281 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.394 kDa
Sequence
MAQHLRKPDWLKIRLGGNEQFTKTKSIVESHCLHTICTSGKCPNMGECWSRGTATFMIGGEICTRSCRFCNTLTGKPLPLDPKEPANVAESIRLMNLKHAVITSVDRDDLPDLGASHWVNTIRTIKEVNPQTTVEVLIPDFQGRLDLVDQVVDAAPEIISHNMETVRRISPQVRSAAKYDVSLSVLRRIAERGVVAKTGIMVGLGETEDEVLELMDDVLQAGVSVLTIGQYLQPSRKNIPVSEYVTPERFEYYRQQAVNKGFKKVESAPLVRSSYHAEKHI

Gene
lipA
Protein
Lipoyl synthase
Organism
Aquifex aeolicus (strain VF5)
Length
276 amino acids
Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Similarity
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Mass
31.785 kDa
Sequence
MMKPVLHFSKLYEVKKLLRKSRLYTVCEESRCPNISECFGNKTATFMILGNRCTRRCAFCNVEKGFPKGVDPEEPYRLLEAVKTLGLKYVVITSVTRDDLPDGGASHFAKCIRVLKENIEDIKVEVLIPDFRGNKKALEVVLKEKPVVLNHNVETVPRLYPSVRIGANYKRSLNILKWSKEIDKSVYTKSALILGFGERKEEVIKVMEDLRSVDCDFLVLGQYYQPSLKHHPVVKYYSEEEFKEFEEIGYEMGFKFVVSKPNARSSYKAFESLLST