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Reviewed, UniProtKB/Swiss-Prot P37941 (ODBB_BACSU)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

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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

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Sequences

Sequence LengthMass (Da)Tools
P37941-1 [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

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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 1-32.
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: 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.

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Cross-references

Sequence databases

M97391 Genomic DNA. Translation: AAA22279.1.
D84432 Genomic DNA. Translation: BAA12599.1.
AL009126 Genomic DNA. Translation: CAB14335.1.
PIRD69593.
RefSeqNP_390284.1.

3D structure databases

HSSPHSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7.
ModBaseSearch...

Genome annotation databases

GeneID938672.
GenomeReviewsGene locus BSU24040 in contig AL009126_GR.
KEGGbsu:BSU24040.
NMPDRfig|224308.1.peg.2408.

Organism-specific databases

SubtiListBG10306. bfmBAB. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP37941.
OMAP37941. NNDWSCP.

Enzyme and pathway databases

BioCycBSUB224308:BSU2402-MON.
MetaCyc:MON-11684.
BRENDA1.2.4.4. 150.

Family and domain databases

InterProIPR005476. Transketo_C.
IPR015941. Transketolase_C-like.
IPR005475. Transketolase_central-reg.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents