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P37940 (ODBA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
2-oxoisovalerate dehydrogenase subunit alpha

EC=1.2.4.4
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
Short name=BCKDH E1-alpha
Gene names
Name:bfmBAA
Synonyms:bfmB1a
Ordered Locus Names:BSU24050
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. 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 structure

Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex.

Sequence similarities

Belongs to the BCKDHA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3303302-oxoisovalerate dehydrogenase subunit alpha
PRO_0000162248

Regions

Region72 – 743Thiamine pyrophosphate binding By similarity
Region107 – 1104Substrate binding By similarity
Region123 – 1253Thiamine pyrophosphate binding By similarity
Region153 – 1597Thiamine pyrophosphate binding By similarity
Region183 – 1875Thiamine pyrophosphate binding By similarity

Sites

Metal binding1541Magnesium By similarity
Metal binding1831Magnesium By similarity
Metal binding1851Magnesium; via carbonyl oxygen By similarity
Binding site441Substrate By similarity
Binding site731Substrate By similarity
Binding site1231Substrate By similarity
Binding site2521Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P37940 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 39584D3F4363E656

FASTA33036,334
        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 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of branched-chain alpha-oxo acid dehydrogenase from Bacillus subtilis and its similarity to other alpha-oxo acid dehydrogenases."
Wang G.-F., Kuriki T., Roy K.L., Kaneda T.
Eur. J. Biochem. 213:1091-1099(1993) [PubMed: 8504804] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22.
Strain: 168.
[2]"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
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. expand/collapse author list , 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.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97391 Genomic DNA. Translation: AAA22278.1.
D84432 Genomic DNA. Translation: BAA12598.1.
AL009126 Genomic DNA. Translation: CAB14336.1.
PIRC69593.
RefSeqNP_390285.1. NC_000964.3.

3D structure databases

ProteinModelPortalP37940.
SMRP37940. Positions 8-330.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002078; EBBACP00000002078; EBBACG00000002075.
GeneID938674.
GenomeReviewsGene locus BSU24050 in contig AL009126_GR.
KEGGbsu:BSU24050.
NMPDRfig|224308.1.peg.2409.
PATRIC18976638. VBIBacSub10457_2509.

Organism-specific databases

GenoListBSU24050. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001071.
HOGENOMHBG753263.
OMADYVLPYY.
PhylomeDBP37940.
ProtClustDBCLSK2752445.

Enzyme and pathway databases

BioCycBSUB:BSU24050-MONOMER.
MetaCyc:MONOMER-11683.

Family and domain databases

InterProIPR001017. DH_E1.
[Graphical view]
KOK00166.
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODBA_BACSU
AccessionPrimary (citable) accession number: P37940
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families