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P37941 (ODBB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-oxoisovalerate dehydrogenase subunit beta

EC=1.2.4.4
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
Short name=BCKDH E1-beta
Gene names
Name:bfmBAB
Synonyms:bfmB1b
Ordered Locus Names:BSU24040
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length327 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 ODBA in the E1 complex.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3273272-oxoisovalerate dehydrogenase subunit beta
PRO_0000162250

Regions

Region58 – 603Thiamine pyrophosphate By similarity
Region83 – 864Substrate By similarity
Region86 – 894Thiamine pyrophosphate By similarity

Sites

Active site1291Proton acceptor By similarity
Binding site291Thiamine pyrophosphate By similarity
Binding site821Thiamine pyrophosphate By similarity
Binding site1291Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P37941 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: F19F5BF8F413EBFE

FASTA32735,856
        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 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-32.
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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97391 Genomic DNA. Translation: AAA22279.1.
D84432 Genomic DNA. Translation: BAA12599.1.
AL009126 Genomic DNA. Translation: CAB14335.1.
PIRD69593.
RefSeqNP_390284.1. NC_000964.3.

3D structure databases

ProteinModelPortalP37941.
SMRP37941. Positions 2-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP37941. 2 interactions.
STRING224308.BSU24040.

Proteomic databases

PaxDbP37941.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14335; CAB14335; BSU24040.
GeneID938672.
KEGGbsu:BSU24040.
PATRIC18976636. VBIBacSub10457_2508.

Organism-specific databases

GenoListBSU24040. [Micado]

Phylogenomic databases

eggNOGCOG0022.
HOGENOMHOG000281451.
KOK00167.
OMAFDTPYPY.
OrthoDBEOG6JQH4C.
ProtClustDBCLSK873415.

Enzyme and pathway databases

BioCycBSUB:BSU24040-MONOMER.
MetaCyc:MONOMER-11684.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODBB_BACSU
AccessionPrimary (citable) accession number: P37941
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 13, 2013
This is version 97 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