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UniProtKB/Swiss-Prot entry P37941


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

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Entry information
Entry name ODBB_BACSU
Primary accession number P37941
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    September 2, 2008 (Entry version 64)
Name and origin of the protein
Protein name 2-oxoisovalerate dehydrogenase subunit beta
Synonyms EC 1.2.4.4
Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
BCKDH E1-beta
Gene name
Name: bfmBAB
Synonyms: bfmB1b
OrderedLocusNames: BSU24040
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 1-32.
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 ODBA in the E1 complex.
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; AAA22279.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D84432; BAA12599.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99116; CAB14335.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D69593; D69593.
RefSeq NP_390284.1; -.
3D structure databases
HSSP Q8ZUR7; 1IK6. [HSSP ENTRY / PDB]
ModBase P37941.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2402-MON; -.
MetaCyc:MON-11684; -.
Organism-specific databases
SubtiList BG10306; bfmBAB. [Micado]
Family and domain databases
InterPro IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.
BLOCKS P37941.
Genome annotation databases
GeneID 938672; -.
GenomeReviews AL009126_GR; BSU24040.
KEGG bsu:BSU24040; -.
NMPDR fig|224308.1.peg.2408; -.
Phylogenomic databases
HOGENOM P37941; -.
Genome annotation databases
CMR P37941; BSU24040.
Other
ProtoNet P37941.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Oxidoreductase; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   327  327     2-oxoisovalerate dehydrogenase subunit beta. PRO_0000162250
REGION   58    60  3     Thiamine pyrophosphate (By similarity). 
REGION   83    86  4     Substrate (By similarity). 
REGION   86    89  4     Thiamine pyrophosphate (By similarity). 
ACT_SITE   129   129        Proton acceptor (By similarity). 
BINDING   29    29        Thiamine pyrophosphate (By similarity). 
BINDING   82    82        Thiamine pyrophosphate (By similarity). 
BINDING   129   129        Substrate (By similarity). 
Sequence information
Length: 327 AA [This is the length of the unprocessed precursor] Molecular weight: 35856 Da [This is the MW of the unprocessed precursor] CRC64: F19F5BF8F413EBFE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVMSYIDAI NLAMKEEMER DSRVFVLGED VGRKGGVFKA TAGLYEQFGE ERVMDTPLAE 

        70         80         90        100        110        120 
SAIAGVGIGA AMYGMRPIAE MQFADFIMPA VNQIISEAAK IRYRSNNDWS CPIVVRAPYG 

       130        140        150        160        170        180 
GGVHGALYHS QSVEAIFANQ PGLKIVMPST PYDAKGLLKA AVRDEDPVLF FEHKRAYRLI 

       190        200        210        220        230        240 
KGEVPADDYV LPIGKADVKR EGDDITVITY GLCVHFALQA AERLEKDGIS AHVVDLRTVY 

       250        260        270        280        290        300 
PLDKEAIIEA ASKTGKVLLV TEDTKEGSIM SEVAAIISEH CLFDLDAPIK RLAGPDIPAM 

       310        320 
PYAPTMEKYF MVNPDKVEAA MRELAEF 

P37941 in FASTA format

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