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UniProtKB/Swiss-Prot entry P37940


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODBA_BACSU
Primary accession number P37940
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on October 1, 1994 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 63)
Name and origin of the protein
Protein name 2-oxoisovalerate dehydrogenase subunit alpha
Synonyms EC 1.2.4.4
Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
BCKDH E1-alpha
Gene name
Name: bfmBAA
Synonyms: bfmB1a
OrderedLocusNames: BSU24050
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-22.
STRAIN=168;
PubMed=8504804 [NCBI, ExPASy, EBI, Israel, Japan]
Wang G.-F., Kuriki T., Roy K.L., Kaneda T.;
"The primary structure of branched-chain alpha-oxo acid dehydrogenase from Bacillus subtilis and its similarity to other alpha-oxo acid dehydrogenases.";
Eur. J. Biochem. 213:1091-1099(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / JH642;
PubMed=8969508 [NCBI, ExPASy, EBI, Israel, Japan]
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.;
"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes.";
Microbiology 142:3103-3111(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
Comments
  • FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
  • CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • SUBUNIT: Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex.
  • SIMILARITY: Belongs to the BCKDHA family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M97391; AAA22278.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D84432; BAA12598.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99116; CAB14336.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C69593; C69593.
RefSeq NP_390285.1; -.
3D structure databases
HSSP P12694; 1DTW. [HSSP ENTRY / PDB]
ModBase P37940.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2403-MON; -.
MetaCyc:MON-11683; -.
Organism-specific databases
SubtiList BG10307; bfmBAA. [Micado]
Ontologies
GO
GO:0003863; Molecular function: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR001017; DHase_E1.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS P37940.
Genome annotation databases
GeneID 938674; -.
GenomeReviews AL009126_GR; BSU24050.
KEGG bsu:BSU24050; -.
NMPDR fig|224308.1.peg.2409; -.
Phylogenomic databases
HOGENOM P37940; -.
Genome annotation databases
CMR P37940; BSU24050.
Other
ProtoNet P37940.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Magnesium; Metal-binding; Oxidoreductase; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   330  330     2-oxoisovalerate dehydrogenase subunit alpha. PRO_0000162248
REGION   72    74  3     Thiamine pyrophosphate binding (By similarity). 
REGION   107   110  4     Substrate binding (By similarity). 
REGION   123   125  3     Thiamine pyrophosphate binding (By similarity). 
REGION   153   159  7     Thiamine pyrophosphate binding (By similarity). 
REGION   183   187  5     Thiamine pyrophosphate binding (By similarity). 
METAL   154   154        Magnesium (By similarity). 
METAL   183   183        Magnesium (By similarity). 
METAL   185   185        Magnesium (via carbonyl oxygen) (By similarity). 
BINDING   44    44        Substrate (By similarity). 
BINDING   73    73        Substrate (By similarity). 
BINDING   123   123        Substrate (By similarity). 
BINDING   252   252        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 330 AA [This is the length of the unprocessed precursor] Molecular weight: 36334 Da [This is the MW of the unprocessed precursor] CRC64: 39584D3F4363E656 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTNRHQALG LTDQEAVDMY RTMLLARKID ERMWLLNRSG KIPFVISCQG QEAAQVGAAF 

        70         80         90        100        110        120 
ALDREMDYVL PYYRDMGVVL AFGMTAKDLM MSGFAKAADP NSGGRQMPGH FGQKKNRIVT 

       130        140        150        160        170        180 
GSSPVTTQVP HAVGIALAGR MEKKDIAAFV TFGEGSSNQG DFHEGANFAA VHKLPVIFMC 

       190        200        210        220        230        240 
ENNKYAISVP YDKQVACENI SDRAIGYGMP GVTVNGNDPL EVYQAVKEAR ERARRGEGPT 

       250        260        270        280        290        300 
LIETISYRLT PHSSDDDDSS YRGREEVEEA KKSDPLLTYQ AYLKETGLLS DEIEQTMLDE 

       310        320        330 
IMAIVNEATD EAENAPYAAP ESALDYVYAK 

P37940 in FASTA format

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