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pdhB

Gene
pdhB
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Length
553 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
56.582 kDa
Sequence
MSQAIEIKVPDIGDYDAVPVIEVHVKPGDSINAEDALVTLESDKATMDVPSPQAGVVKDVRIKVGDNVSEGSVLVMLEAANEPAAAPAPAAAAPAPAAAAPAPAPAPAAAPAAAPAAGGGGTIEVKVPDIGDYDAVPVIEVHVKAGDTINAEDAVVTLESDKATMDVPSPQGGVVKEVKVKVGDNVAEGTLLLILEGAAASAAPAAAAAAPAPAASAPAPAPAPAAAAPAPAAAPAAAPAAAGVTGKAAHASPSVRKFARELGVDVSRVPGTGPKGRITQEDVQGYVKGVMSGQAAAPAQAAAAGAGGGELGLLPWPKFDFTRFGEVESKALSRIKKISGANLHRNWVMIPHVTNHDEADITELEAFRLQLNKENEKSGIKVTMLAFMIKATVAALKKFPNFNASLDGDNLVLKKYFNIGFAADTPNGLVVPVIKDADKKGVLEISQEMSELAKLARDGKLKPDQMQGGCFSISSLGGLGGTYFTPIINAPEVAIMGVCKSYQKPVWDGKQFAPRLTLPLSLSWDHRVIDGAEAARFNTYFGQLLADFRRILL
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Length
462 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).
Mass
49.833 kDa
Sequence
MAIELKMPALSPTMEEGTLTRWLVKEGDSIKAGEILAEIETDKAIMEFEAVDEGVITKILIPEGSENVKVGTAIAYLGTDANDVTLDGASAETKAEESAPVASPAKTEAAAVEEAATPSLGKVINSAPEIPEGTEFFQQTLREALRDAMAEEMRRDDRVFVMGEEVAEYQGAYKVTQGLLQEFGARRVVDTPISEYGFSGIGVGAAMEGLRPVIEFMTMNFSMQAIDHIINSAAKTHYMSGGQVRCPIVFRGPNGAAPRVGAQHTQNFGPWYAAVPGLVVLAPYDAIDAKGLLKAAIRSDDPVVFLECELLYGKTFDVPKMDDFVLPIGKARIIREGKDVTIVSYSIGVSFALTAAEALAKEGIDAEVIDLRTLRPLDKETILQSLAKTNRIVTVEDGWPVCSISSEIAAIAMEEGFDNLDAPVLRVTNADTPTPYAENLEKKGLVNPEAIIEAVRKVCYRK
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Rhizobium meliloti (strain 1021)
Length
460 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).
Mass
48.812 kDa
Sequence
MPVEILMPALSPTMEEGTLSKWLKNEGDKVSSGDVIAEIETDKATMEVEAVDEGTIGKLLIAAGTEGVKVNTPIAVLLQDGEAASDIDSMKTEAPKAETPKPAAAEAPAASAAPVAAQPKADVPSDPAIPAGTEMATMTVREALRDAMAEEMRANEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVVDTPITEHGFAGVGVGAAMTGLRPIVEFMTFNFAMQAIDQIINSAAKTLYMSGGQMGAPIVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPNPVIFLENEILYGQSFEVPKLDDFVLPIGKARIHRTGKDATLVSFGIGMTYAIKAAAELEAQGIDVEIIDLRTIRPMDLPTVIESVKKTGRLVTVEEGYPQSSVGTEIATRVMQQAFDYLDAPILTIAGKDVPMPYAANLEKLALPNVAEVVDAVKAVCYK
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
PDHB
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Organism
Bos taurus
Length
359 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Mass
39.126 kDa
Sequence
MAVVAVLVRKPLEQVSGLLRRRFHRTAPAALQVTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSGGLQSVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWSSEDAKGLIKSAIRDNNPVVVLENELMYGVPFELPSEAQSKDFLIPIGKAKIERQGTHVTIVAHSRPVGHCLEAATVLSKEGIECEVINLRTIRPMDIETIEGSVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSVPQVKDIIFAIKKTLNI
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial: PDHB

Gene
PDHB
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Organism
Homo sapiens
Length
359 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Mass
39.233 kDa
Sequence
MAAVSGLVRRPLREVSGLLKRRFHWTAPAALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial: PDHB

Gene
Pdhb
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Organism
Mus musculus
Length
359 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Mass
38.937 kDa
Sequence
MAVVAGLVRGPLRQASGLLKRRFHRSAPAAVQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVMLENELMYGVAFELPAEAQSKDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKVLEDNSVPQVKDIIFAVKKTLNI
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial: Pdhb

Gene
PDHB
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Organism
Pongo abelii
Length
359 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Mass
39.333 kDa
Sequence
MAAVSGLVRRPLREVSRLLKRRFHWTAPAALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial: PDHB

Gene
Pdhb
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Organism
Rattus norvegicus
Length
359 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Mass
38.982 kDa
Sequence
MAAVAGLVRGPLRQASGLLKRRFHRSAPAAVQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVMLENELMYGVAFELPTEAQSKDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial: Pdhb

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Organism
Dictyostelium discoideum
Length
356 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).
Mass
39.068 kDa
Sequence
MLSSILKKIQPSLLVNFRIITRTYATKEVTVRDAINSALDEELARDEKVFIMGEEVAQYNGAYKITKGLFDKYGGDRIIDTPITEAGFAGIGVGAAMAGTRPIIEFMTFNFAMQAIDHIINSSAKTHYMSGGKVFNPIVWRGPNGPPTAVGAQHSQCFAAWYGSVPGLKVVAPWSAADHRGLLKSAIRDDNPVVYLESELLYNYKFDLSDQEQDKEYLVPIGKAKVEREGKDVTIVGFSRIVSNCMEAAEILAKEGISAEVINLRTIRPIDAETIVNSLKKTNKLVTVEEGWAQSGIGAEISALMMEHAFDYLDAPIERICGADVPMPYASNLENAAMVQTQNIVNAAKRVTQRNK
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
Length
337 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).
Mass
36.087 kDa
Sequence
MERAPALAEPEPRVQSLPMVKALNAGLRQALVADPKVLILGEDVGPLGGVFRVTEGLQSEFGASRVVDTPLAEAGIVGTAIGLAMRGYRPVVEIQFNGFVFPGFDQITTQLAKMANRHSGAVSMPVVIRIPHGGHIGAVEHHQEAPEAYFAHTAGLRIVAPSTPHDAYWMIQEAIASDDPVIFFEPMSRYWPKGEVDTLENPLPLHASRIVRSGTDATIVAWAGMVPVALRAAEIAAEEGRSLEVVDLRSLAPIDYAPVLRSVQKTGRLVVAQEAPGIVSVGSEVAAVVGEKAFYSLEAPVLRVAGFDTPFPPAKLESLYLPDADRILEVVDRSLAY
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Chlorokybus atmophyticus
Length
335 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).
Mass
36.68 kDa
Sequence
MAVRFLFEALQKAIDEEMEREKRVVLIGEDIGHYGGSYKVTQGLYGKYGKHRVIDTPIAEYSFVGAAVGAAATGLIPVVEGMNMAFILLAYSQISNNMGMLCATSGGHFQVPMVLRGPGGIGKQLGAEHSQRLESYFQSVPGLQIVTCSTPYNAKGLLKSAIRSKNPILFIEHVLLYNLKGEVPDNDYLLPLEKAELVREGSDITVLTYSRQRYNVIQAVKVLVEEGYDPEVIDLISLKPFDMETIGKSIQKTHKVLIVEECMMTGGISNVLQSLIIDNFFDALDAAPLILSSPNVPTPYTGPLEEATVVQTIDIIESIEYGITGKPPKPRTAKK
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Porphyra purpurea
Length
331 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).
Mass
36.394 kDa
Sequence
MSKVFMFDALRAATDEEMEKDLTVCVIGEDVGHYGGSYKVTKDLHSKYGDLRVLDTPIAENSFTGMAIGAAITGLRPIVEGMNMSFLLLAFNQISNNAGMLRYTSGGNFTLPLVIRGPGGVGRQLGAEHSQRLEAYFQAIPGLKIVACSTPYNAKGLLKSAIRDNNPVVFFEHVLLYNLQEEIPEDEYLIPLDKAEVVRKGKDITILTYSRMRHHVTEALPLLLNDGYDPEVLDLISLKPLDIDSISVSVKKTHRVLIVEECMKTAGIGAELIAQINEHLFDELDAPVVRLSSQDIPTPYNGSLEQATVIQPHQIIDAVKNIVNSSKTITT
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Pyropia yezoensis
Length
331 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).
Mass
36.385 kDa
Sequence
MSKIFMFDALRAATDEEMAKDPTVCVIGEDVGHYGGSYKVTKDLHSKYGDLRVLDTPIAENSFTGMAIGAAITGLRPIVEGMNMSFLLLAFNQISNNAGMLRYTSGGNFTLPLVIRGPGGVGRQLGAEHSQRLEAYFQAIPGLKIVACSTPYNAKGLLKSAIRDNNPVVFFEHVLLYNLQEEIPQEEYFLPLNKVEFVRKGKDITILTYSRMRHHVIQALPALLKEGYDPEVIDLISLKPLDIDSISISVKKTHKVLIVEECMKTAGIGAELIAQINEYLFDELDAPVVRLSSQDIPTPYNGSLEQATVIQPSQIVDSVKSIITSVKAIIT
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staurastrum punctulatum
Length
328 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).
Mass
35.943 kDa
Sequence
MSEMLLFEALREGLQEEMDRDPKVLVMGEDVGHYGGSYKVTKGFAEKYGDLRLLDTPIAENSFTGMAIGAAMTGLRPVVEGMNMGFLLLAFNQIANNAGMLHYTSGANFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQLVACSTPINAKGLIKSSIRSENPVILFEHVLLYNLKETIPDNEYLVCLEKAEIVRPGTDITILTYSRMRHHVLQATKSLVYKGYDPEIIDIVSLKPVDLGTISTSIKKTHKVLIVEECMRTGGIGASLRATIMEHLFDFLDAPIMCLSSQDVPTPYSGPLEELTVIQPAQIVQAVEQLCNNGNN
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Acholeplasma laidlawii
Length
327 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).
Mass
35.682 kDa
Sequence
MAIITLLEAINQAIDQAMEKDESIVVFGEDAGFEGGVFRVTAGLQKKYGETRVFDTPIAESAIVGSAVGMAINGLKPIAEIQFDGFIFPGYTDLVTHAARMRNRSRGQFTVPMVLRLPHGGGIRALEHHSEALEVLFGSIPGLKVVTPSTPYDAKGLLLAAINDPDPVVFLEPKRIYRAGKQEVPAEMYEIPIGKAKVVKQGTDMTVVAWGSIVREVEKAVKLVEAEGISVEIIDLRTISPIDEETILNSVKKTGKFMVVTEAVKSYGPAAELITMVNEKAFFHLEAAPVRFTGFDITVPLARGEHYHFPQPEKIAAYIRKLAKARP
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Cyanidium caldarium
Length
327 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).
Mass
35.946 kDa
Sequence
MSMMFLYEALRAAIDEEMGKDSNVFIVGEDVGHYGGSYKVTKDLHVKYGDLRVLDAPIAENSFTGMAIGAAMTGLRPIVEGMNMGFMLLAFNQISNNLSMLQYTSGGNFNIPVVIRGPGGIGKQLAAEHSQRLESCFQSIPGLQIVACSTAYNAKGLLKSAIIEKKPILFLEHVLLYNLKGFVPDEEYYLPLDKAEVVRSGSDVTIVTYSRMRYHVLAAVEKLVLNGQDPEIIDLISLKPLDLHTISKSIKKTHKIVIVEECAQTGGIAAELISLINTYLYDELDSPAVRLSSKDVPIPYNGNLEKSTLIQPDQIVDVVTNLLQYKT
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Mesostigma viride
Length
327 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).
Mass
36.005 kDa
Sequence
MTVRFLFEALNMAIDEEMARNDKVALLGEDIGHYGGSYKVTQNLYAKYGEHRVIDTPIAENSFVGAAIGAAMTGLVTVVEGMNMGFILLAFSQISNNMGMLSATSGGHYHIPIVLRGPGGVGKQLGAEHSQRLECYFQSVPGLQIVACSTPYNAKGLLKSAIRSKNPIFFLEHVLLYNLKAEVPDNDYVLPLEKAEIVRQGNDITILTYSRMRYNVIQAVKVLVEKGYDPEIIDLISLKPFDIETIGKSIQKTHKVLIVEESMMTGGISNVLQSLILENFFDDLDNRPMCLSSPNVPTPYSGPLEEVSIVQTADIIESVEQILTNKM
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Length
327 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).
Mass
35.914 kDa
Sequence
MSKTIQANNIEALGNAMDLALERDPNVVLYGQDAGFEGGVFRATKGLQKKYGEERVWDCPIAEAAMAGIGVGAAIGGLKPIVEIQFSGFSFPAMFQIFTHAARIRNRSRGVYTCPIIVRMPMGGGIKALEHHSETLEAIYGQIAGLKTVMPSNPYDTKGLFLAAVESPDPVVFFEPKKLYRAFRQEIPADYYTVPIGQANLISQGNNLTIVSYGPTMFDLINMVYGGELKDKGIELIDLRTISPWDKETVFNSVKKTGRLLVVTEAAKTFTTSGEIIASVTEELFSYLKAAPQRVTGWDIVVPLARGEHYQFNLNARILEAVNQLLK
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Chaetosphaeridium globosum
Length
326 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).
Mass
35.969 kDa
Sequence
MAEVLLFEALRDALDEEMQRDPSVLVMGEDVGHYGGSYKVTKGFHEKYGDLRLLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFLLLAFNQIANNAGMLHYTSGGNFKIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQMVACSTPYNGKGLLKSAIRNDNPVIFFEHVLLYNLNENLIEQEYLLCLEKAEVVRPGNDITILTYSRMRHHVLQAAKVLVNKGYDPEIIDILSLKPLDMGTISLSVRKTHKVLIVEECMRTGGIGASLRAAILEDLFDYLDAPIQCLSSQDVPTPYSGPLEELTVIQPNQIIQAVEEMCKIE
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Chara vulgaris
Length
326 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).
Mass
36.005 kDa
Sequence
MSEKLLYEALNEGIHEEIERDPKVFVIGEDIGHYGGSYKVTKGLFEKYGNLRILDTPIAENSFTGIAIGAAMTGLRPIIEGMNMGFLLLAFNQIANNAGMLHYTSGGNFTTPLVVRGPGGVGRQLGAEHSQRLESYFQSVPGLQMVACSTPYNAKGLIKSAIRSQNPIIFFEHVLLYNIKENIPQKEYLVPLEKAELVRSGNQITILTYSRMRYHVLQAAKTLIEKGYDPEIIDIISLKPLDMGTISTSLRKTHKVLIVEECMKTGGIGTTLKSAILESLFDFLDTPIMSLSSQDVPTPYNGFLEDLTVIQPSQIVEAAEKIILYS
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
Length
326 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).
Mass
35.761 kDa
Sequence
MQITVREALRDAMQEEMIRDDKVFVMGEEVAEYQGAYKVTQGLLEQFGPKRVIDTPITEYGFAGLAVGAAFAGLRPIVEFMTFNFAMQAFDHIVNSAAKTHYMSGGQAKCPIVFRGPNGAASRVAAQHSQNYTACYSHVPGLKVVAPYSAEDHKGLMLTAIRDDNPVIFLENEILYGHSFDVPETIEPIPFGQAKILREGSSVTIVTFSIQVKLALDAANVLQNDNIDCEVIDLRTIKPLDTDTIIESVKKTNRLVIVEEGWFFAGVGASIASIVMKEAFDYLDAPIEIVSGKDVPLPFAVNLEKLALPSESDVIEAVKKVCYYSV
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Rickettsia prowazekii (strain Madrid E)
Length
326 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).
Mass
35.917 kDa
Sequence
MQITVREALRDAMQEEMLRDEKVFVIGEEVAEYQGAYKVTQGLLEQFGSKRVIDTPITEYGFAGLAVGAAFAGLRPIVEFMTFNFAMQAFDHIVNSAAKTHYMSGGQVKCPIVFRGPNGAASRVAAQHSQNYTACYSHIPGLKVVAPYSAEDHKGLMLTAIRDDNPVIFLENEILYGHSFDVPDIIEPIPFSKAKILKEGSNVTIVTFSIQVKLALDVVNILQNDNIDCELIDLRTIKPLDTDSIIESVKKTNRLVIVEEGWFFAGVGASIASIVMKEAFDYLDAPIEIVSGKDVPLPYAVNLEKLAMPSANDLIEAVKKVCYYSI
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Rickettsia typhi (strain ATCC VR-144 / Wilmington)
Length
326 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).
Mass
35.961 kDa
Sequence
MQITVREALRDAMQEEMLRDDKVFVIGEEVAEYQGAYKVTQGLLEQFGSKRVIDTPITEYGFAGLAVGAAFAGLRPIVEFMTFNFAMQAFDHIVNSAAKTHYMSGGQVKCPIVFRGPNGAASRVAAQHSQNYTACYSHIPGLKVVAPYSAEDHKGLMLTAIRDDNPVIFLENEILYGHSFDVPDIIEPIPFSKAKILKEGSNVTIVTFSIQVKLALDVVNILQNDNIDCELIDLRTIKPLDTNMIIESVKKTNRLVIVEEGWFFAGVGASIASIVMKEAFDYLDAPIEIVSGKDVPLPYAVNLEKLAMPSANDLIEAVKKVCYYTI
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Cyanidioschyzon merolae (strain 10D)
Length
326 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).
Mass
35.983 kDa
Sequence
MLHKLFMYEALREAIDEEMARDKRVFVLGEDVGHYGGSYKVTKQLHTKYGDLRVLDTPIAENSFTGMAIGAAMTGLKPVVEGMNLSFLLLAFNQISNNAGMLHYTSGGNWSIPLVIRGPGGIGKQLSAEHSQRIEAYFQAVPGLKIVACSTPYNAKGLLKAAIRDNNPVLFLEHVLLYNLKQEIPKQEYVLPLDKAQVVREGSDVTIITYSRMLHHVMQAVKQLVAQGMNPEVIDLISLKPIDLETLVTSVSKTHKAIIVEECMQTGGIAAEVMAQIYSHAFDELDAPIRRLSSKDVPTPYNGYLEQACLVQPTQIVEAVKTLMST
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Length
326 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).
Mass
36.026 kDa
Sequence
MSKIQVNNIEALNNAMDLALERDQNVVLYGQDAGFEGGVFRATKGLQQKYGSERVWDCPIAENSMAGIGVGAAIGGLKPIVEIQFSGFSFPAMFQIFVHAARIRNRSRGVYTAPLVVRMPMGGGIKALEHHSETLEAIYAQIAGLKTVMPSNPYDTKGLFLAAIESPDPVIFFEPKKLYRAFRQEIPSDYYTVPIGEANLISEGSELTIVSYGPTMFDLINLVYSGELKDKGIELIDLRTISPWDKQTVFNSVKKTGRLLVVTEAVKSFTTSAEIITSVTEELFTYLKKAPQRVTGFDIVVPLARGEKYQFEINARVIDAVNQLLK
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Length
326 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).
Mass
35.821 kDa
Sequence
MQITVREALRDAMQEEMIRDDKVFVIGEEVAEYQGAYKVTQGLLEQFGPKRVIDTPITEYGFAGLAVGAAFAGLRPIVEFMTFNFAMQAFDHIVNSAAKTHYMSGGQVKCPIVFRGPNGAASRVAAQHSQNYTACYSHIPGLKVVAPYSAEDHKGLMLTAIRDDNPVVFLENEILYGHSFDVPKTIEPIPFGQAKILREGSSVTIVTFSIQVKLALDAANFVQNDNIDCEVIDLRTIKPLDTETIIESVKKTNRLVVVEEGWFFAGVGASIASIVMKEAFDYLDAPIEIVSGKDLPLPYAVNLETLALPSESDVIEAVKKVCYYSI
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Bacillus subtilis (strain 168)
Length
325 amino acids
Function
The B.subtilis PDH complex possesses also branched-chain 2-oxoacid dehydrogenase (BCDH) activity.
Mass
35.474 kDa
Sequence
MAQMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVMEIQFFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLISAIRDNDPVVFLEHMKLYRSFRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAADELEKDGISAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFSQAESVWLPNHKDVLETARKVLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staphylococcus aureus (strain COL)
Length
325 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).
Mass
35.216 kDa
Sequence
MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRGPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
325 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).
Mass
35.246 kDa
Sequence
MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRSPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staphylococcus aureus (strain N315)
Length
325 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).
Mass
35.246 kDa
Sequence
MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRSPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staphylococcus aureus (strain MRSA252)
Length
325 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).
Mass
35.246 kDa
Sequence
MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRSPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staphylococcus aureus (strain MSSA476)
Length
325 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).
Mass
35.246 kDa
Sequence
MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRSPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staphylococcus aureus
Length
325 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).
Mass
35.246 kDa
Sequence
MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRSPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staphylococcus aureus (strain MW2)
Length
325 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).
Mass
35.246 kDa
Sequence
MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRSPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Length
325 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).
Mass
35.293 kDa
Sequence
MAQMTMVQAINDALKSELKRDEDVLVFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLAVTGFRPVMEIQFLGFVYEVFDEVAGQIARTRFRSGGTKPAPVTIRTPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIQSNDPVVYLEHMKLYRSFREEVPEEEYKIDIGKANVKKEGNDITLISYGAMVQESLKAAEELEKDGYSVEVIDLRTVQPIDIDTLVASVEKTGRAVVVQEAQRQAGVGAQVAAELAERAILSLEAPIARVAASDTIYPFTQAENVWLPNKKDIIEQAKATLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Length
325 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).
Mass
35.293 kDa
Sequence
MAQMTMVQAINDALKSELKRDEDVLVFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLAVTGFRPVMEIQFLGFVYEVFDEVAGQIARTRFRSGGTKPAPVTIRTPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIQSNDPVVYLEHMKLYRSFREEVPEEEYKIDIGKANVKKEGNDITLISYGAMVQESLKAAEELEKDGYSVEVIDLRTVQPIDIDTLVASVEKTGRAVVVQEAQRQAGVGAQVAAELAERAILSLEAPIARVAASDTIYPFTQAENVWLPNKKDIIEQAKATLEF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Zygnema circumcarinatum
Length
325 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).
Mass
35.808 kDa
Sequence
MAEVLLFEALRQGLQEEMDRDPRVMVMGEDVGHYGGSYKVTKGFAERYGDLRLLDTPIAENSFTGMAIGAAMTGLRPVVEGMNMGFLLLAFNQIANNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQMVACSTPYNAKGLIKSAIRSDNPIILFEHVLLYNLKEDLAEEEYLVCLEKAEVVRPGNDITILTYSRMRHNVLQATKSLVYKGYDPEIIDIVSLKPFDLGTIGASVCKTHKVLIVEECMRTGGIGATLRAAIMEHFFDYLDAPILCLSSQDVPTPYSSPLEELTVIQPNQIIQVVEQLCEN
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Geobacillus stearothermophilus
Length
325 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).
Mass
35.46 kDa
Sequence
MAQMTMVQAITDALRIELKNDPNVLIFGEDVGVNGGVFRATEGLQAEFGEDRVFDTPLAESGIGGLAIGLALQGFRPVPEIQFFGFVYEVMDSICGQMARIRYRTGGRYHMPITIRSPFGGGVHTPELHSDSLEGLVAQQPGLKVVIPSTPYDAKGLLISAIRDNDPVIFLEHLKLYRSFRQEVPEGEYTIPIGKADIKREGKDITIIAYGAMVHESLKAAAELEKEGISAEVVDLRTVQPLDIETIIGSVEKTGRAIVVQEAQRQAGIAANVVAEINERAILSLEAPVLRVAAPDTVYPFAQAESVWLPNFKDVIETAKKVMNF
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Rickettsia bellii (strain RML369-C)
Length
325 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).
Mass
35.708 kDa
Sequence
MQITVREALRDAMQEEMIRDDKVFVMGEEVAEYQGAYKVTQGLLEQFGPKRVIDTPITEYGFAGLAVGAAFAGLRPIVEFMTFNFAMQAMDHIVNSAAKTHYMSGGQVRCPIVFRGPNGAASRVAAQHSQNYAACYSYIPGLKVVAPYSAEDHKGLMITAIRDDNPVIFLENEILYGHSFDISENVEPIPFGKAKVLKEGDSVTIVTFSIQVKLALDAANILQSDNINCEVIDLRTIKPLDIDTIIESVKKTGRLVVIEEGWFFAGIGATIAAIVMKEAFDYLDAPVEIVSGKDVPLPYAVNLEKLALPSEYDVINAVKKVCYIK
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
pdhB
Protein
Pyruvate dehydrogenase E1 component subunit beta
Organism
Gracilaria tenuistipitata var. liui
Length
323 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).
Mass
35.742 kDa
Sequence
MTEVLMFDALREATDEEMQNDSSVFILGEDVGHYGGSYKVTKDLHSKYGDLRVLDTPIAENSFMGMAIGAAITGLRPIVEGMNMSFLLLAFNQISNNAGMLRYTSGGNFQIPIVIRGPGGVGRQLGAEHSQRLEAYFQAIPGLKIVACSTPYNAKGLLKSAIRDNNPVIFFEHVLLYNLKDELPNDEYFLPLDKAELVRDGLDVTILTYSRMRHHVMQAVVDLVNDGYNPEVIDLISLKPLDITSIAQSLMKTHKLIIVEECMKTGGIGAEIIAQINDNYFDFLDAPIVRLSSQDIPTPYNGKLEKATVIYPQQIIEAVKSIV
Protein
Pyruvate dehydrogenase E1 component subunit beta: pdhB

Gene
PDHB
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Organism
Mesocricetus auratus
Length
211 amino acids
Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Mass
23.01 kDa
Fragment
multiple
Sequence
EAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVMLENELMYGVAFELPTEAQSKDFLIPIGKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAK
Protein
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial: PDHB