About Products Protein Database Contact

aceF

Gene
aceF
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Length
675 amino acids
Function
Is essential for both 2-oxoglutarate dehydrogenase (ODH) and pyruvate dehydrogenase (PDH) activities, but AceF has exclusively transacetylase (and no transsuccinylase) activity. The lipoyl residues required for ODH activity are likely provided by AceF.
Similarity
Belongs to the 2-oxoacid dehydrogenase family.
Mass
70.905 kDa
Sequence
MAFSVEMPELGESVTEGTITQWLKSVGDTVEVDEPLLEVSTDKVDTEIPSPVAGVILEIKAEEDDTVDVGGVIAIIGDADETPANEAPADEAPAPAEEEEPVKEEPKKEAAPEAPAATGAATDVEMPELGESVTEGTITQWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTVDVGAVIARIGDANAAAAPAEEEAAPAEEEEPVKEEPKKEAAPEAPAATGAATDVEMPELGESVTEGTITQWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTIVEILADEDDTVDVGAVIARIGDANAAAAPAEEEAAPAEEEEPVKEEPKKEEPKKEEPKKEAATTPAAASATVSASGDNVPYVTPLVRKLAEKHGVDLNTVTGTGIGGRIRKQDVLAAANGEAAPAEAAAPVSAWSTKSVDPEKAKLRGTTQKVNRIREITAMKTVEALQISAQLTQLHEVDMTRVAELRKKNKPAFIEKHGVNLTYLPFFVKAVVEALVSHPNVNASFNAKTKEMTYHSSVNLSIAVDTPAGLLTPVIHDAQDLSIPEIAKAIVDLADRSRNNKLKPNDLSGGTFTITNIGSEGALSDTPILVPPQAGILGTGAIVKRPVVITEDGIDSIAIRQMVFLPLTYDHQVVDGADAGRFLTTIKDRLETANFEGDLQL

Gene
aceF
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Organism
Escherichia coli (strain K12)
Length
630 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Similarity
Belongs to the 2-oxoacid dehydrogenase family.
Mass
66.096 kDa
Sequence
MAIEIKVPDIGADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTQTGALIMIFDSADGAADAAPAQAEEKKEAAPAAAPAAAAAKDVNVPDIGSDEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAGAAAPAAKQEAAPAAAPAPAAGVKEVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGVVKELKVNVGDKVKTGSLIMIFEVEGAAPAAAPAKQEAAAPAPAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKEAIKRAEAAPAATGGGIPGMLPWPKVDFSKFGEIEEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITELEAFRKQQNEEAAKRKLDVKITPVVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYINIGVAVDTPNGLVVPVFKDVNKKGIIELSRELMTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMLPISLSFDHRVIDGADGARFITIINNTLSDIRRLVM

Gene
aceF
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
567 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Similarity
Belongs to the 2-oxoacid dehydrogenase family.
Mass
59.411 kDa
Sequence
MSKQIQIPDIGSDEVTVTEVMVNVGDTISVDQSIINVEGDKASMEVPAPEAGVVKEILVKVGDKVSTGTPMLVLEAAGAAPAADEPTAPVADAPTAPVVATAPTASAIVEVNVPDIGGDEVNVTEIMVAVGDTITEEQSLITVEGDKASMEVPAPFGGVVKEILVKSGDKVSTGSLIMRFEVLGAAPAESASAPASTSAPQTAAPATTAQAPQAAAPDTTAQAPQAAAPDTTAQAAQSNNNVSGLSQEQVEASTGYAHATPVIRRLAREFGVNLDKVKGTGRKGRIVKEDIEAYVKTAVKAYESGATAQATGNGVANGAGLGLLPWPKVDFSKFGEIEEVELSRINKISGANLHRNWVIIPHVTHFDKADITDLEAFRKEQNALREKQKLGVKITPVVFIMKAVAKALEAYPRFNSSITEDAQRLILKKYINIGVAVDTPNGLVVPVFKNVNKKGIIELSRELMEVSKKAREGKLTASDMQGGCFTISSLGGIGTTHFAPIVNAPEVAILGVSKSSMEPVWNGKEFAPRLILPMSLSFDHRVIDGADGARFISYLGSVLADLRRLVM

Gene
aceF
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
547 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Similarity
Belongs to the 2-oxoacid dehydrogenase family.
Mass
56.709 kDa
Sequence
MSELIRVPDIGNGEGEVIELLVKPGDKVEADQSLLTLESDKASMEIPSPKAGVVKSIKAKVGDTLKEGDEILELEVEGGEQPAEAKAEAAPAQPEAPKAEAPAPAPSESKPAAPAAASVQDIKVPDIGSAGKANVIEVMVKAGDTVEADQSLITLESDKASMEIPSPASGVVESVSIKVGDEVGTGDLILKLKVEGAAPAAEEQPAAAPAQAAAPAAEQKPAAAAPAPAKADTPAPVGAPSRDGAKVHAGPAVRMLAREFGVELSEVKASGPKGRILKEDVQVFVKEQLQRAKSGGAGATGGAGIPPIPEVDFSKFGEVEEVAMTRLMQVGAANLHRSWLNVPHVTQFDQSDITDMEAFRVAQKAAAEKAGVKLTVLPILLKACAHLLKELPDFNSSLAPSGKALIRKKYVHIGFAVDTPDGLLVPVIRDVDRKSLLQLAAEAADLADKARNKKLSADAMQGACFTISSLGHIGGTGFTPIVNAPEVAILGVSKATMQPVWDGKAFQPRLMLPLSLSYDHRVINGAAAARFTKRLGELLADIRTLLL

Gene
aceF
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Length
410 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Similarity
Belongs to the 2-oxoacid dehydrogenase family.
Mass
46.119 kDa
Sequence
MPDIGTDLVEVIEILVKIGDQVKKDDSLITVEGQKASIEIPASHTGTIKNIIVHIGEKITTGSLIAILNGIDDNVKSKNDSSSYSFKNSKNTSTNSNLGNVNNNINNRTILVHATPTVRRLARKFDIKLENITGTGRKGRILKEDVISYKNISLFNDIKKSLKKTNVNYYKDNVTCDDFKSIELTRTQIRSSKNLLKSWLTIPHVTQFDESDITELENFRQKYNSDLKDKSKKLTILIFVIKAVSKALEMFPKFNGRLINKDNRIAIVLNEHINIGIVVDTDDGLLVPVINRVNKKNISSISNDLRIISERARSRKLNFSDIKEYGSFTISNLGGIGGTNFTPIIKYPELAILGISRALIKPYWNSHAFIPKLMLPLSLSYDHRAIDGVAAVRFITFVKKMLTDIRFLMI

Gene
aceF
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Length
402 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Similarity
Belongs to the 2-oxoacid dehydrogenase family.
Mass
45.421 kDa
Sequence
MPDIGLEEVEVTEILVKIGEEIKLDQGLITVEGDKASMEIPSPISGIVKDITIKIGEKVKTSSIIMIFKVNNLNSIKNEKDLNYIKTEKKLNENFLEEKKDIKKIVLVHATPVVRRLARHLNVDLKNITPSGPKNRILKEDIELYIRNNTSNKSSFNIEKNNTTNFHKDLFNEIPITNIQQIIGKNLHQNWVNIPHVTQFDEVNITLLEEFRHKYNTEKKQKNNMCSKITILPFIIKSVAYGLLEFPIFNSSLSVNKKTIFLKKYVNVGIAVDVQNALFVPVLKNVDKKNIANLSSELIFLSKKAHENKLDASDMKDGCFTISNLGGIGGSWFSPIINSPEVAILGVSKALIKPLWNGKEFIPSLMLPLSLSYDHRVINGADAARFLTFIGKMLSDIRFLIM

Gene
aceF
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
Length
396 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Similarity
Belongs to the 2-oxoacid dehydrogenase family.
Mass
45.278 kDa
Sequence
MPDIGLEEVEIIEILVSINEKIAPEQGLITVEGDKTSMEIPSPISGIVKHIFIKIGEKIKTDALIMRCEVENIDFHVKKKEEICLDNNVLNKVEKNFKKDIFFHATPLIRRLARNLNINLYDVVGTGPKNRILKEDLDLYQSNIKENLIEEKNKINFGDSKKSKTKELELSDIQKNIGNNLHRNWMNIPHVTQFDEVDITILEKFRQKYNNEKRNQKKTNENITILVFIIKVVAYALEKFPIFNSSLNINNKKIILKKYINIGFAIDVNNDLFVPVLKDVNKKNIKQLSSELILLSEKARTRKLNIEDMTGGCFTISNLGGIGGSWFSPIINSPEVAILGISKSQIKPSWNGKEFIPSLMLPLSLSYDHRVINGAYAARFITFISRVLSDMHFLIM