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Protein

2-oxoisovalerate dehydrogenase subunit beta

Gene

bfmBAB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291Thiamine pyrophosphateBy similarity
Binding sitei82 – 821Thiamine pyrophosphateBy similarity
Active sitei129 – 1291Proton acceptorBy similarity
Binding sitei129 – 1291SubstrateBy similarity

GO - Molecular functioni

  1. 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciBSUB:BSU24040-MONOMER.
MetaCyc:MONOMER-11684.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:bfmBAB
Synonyms:bfmB1b
Ordered Locus Names:BSU24040
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU24040. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3273272-oxoisovalerate dehydrogenase subunit betaPRO_0000162250Add
BLAST

Proteomic databases

PaxDbiP37941.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP37941. 2 interactions.
STRINGi224308.BSU24040.

Structurei

3D structure databases

ProteinModelPortaliP37941.
SMRiP37941. Positions 2-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 603Thiamine pyrophosphate bindingBy similarity
Regioni83 – 864Substrate bindingBy similarity
Regioni86 – 894Thiamine pyrophosphate bindingBy similarity

Phylogenomic databases

eggNOGiCOG0022.
HOGENOMiHOG000281451.
InParanoidiP37941.
KOiK00167.
OMAiPIAEMQY.
OrthoDBiEOG6JQH4C.
PhylomeDBiP37941.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

P37941-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVMSYIDAI NLAMKEEMER DSRVFVLGED VGRKGGVFKA TAGLYEQFGE
60 70 80 90 100
ERVMDTPLAE SAIAGVGIGA AMYGMRPIAE MQFADFIMPA VNQIISEAAK
110 120 130 140 150
IRYRSNNDWS CPIVVRAPYG GGVHGALYHS QSVEAIFANQ PGLKIVMPST
160 170 180 190 200
PYDAKGLLKA AVRDEDPVLF FEHKRAYRLI KGEVPADDYV LPIGKADVKR
210 220 230 240 250
EGDDITVITY GLCVHFALQA AERLEKDGIS AHVVDLRTVY PLDKEAIIEA
260 270 280 290 300
ASKTGKVLLV TEDTKEGSIM SEVAAIISEH CLFDLDAPIK RLAGPDIPAM
310 320
PYAPTMEKYF MVNPDKVEAA MRELAEF
Length:327
Mass (Da):35,856
Last modified:October 1, 1994 - v1
Checksum:iF19F5BF8F413EBFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97391 Genomic DNA. Translation: AAA22279.1.
D84432 Genomic DNA. Translation: BAA12599.1.
AL009126 Genomic DNA. Translation: CAB14335.1.
PIRiD69593.
RefSeqiNP_390284.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14335; CAB14335; BSU24040.
GeneIDi938672.
KEGGibsu:BSU24040.
PATRICi18976636. VBIBacSub10457_2508.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97391 Genomic DNA. Translation: AAA22279.1.
D84432 Genomic DNA. Translation: BAA12599.1.
AL009126 Genomic DNA. Translation: CAB14335.1.
PIRiD69593.
RefSeqiNP_390284.1. NC_000964.3.

3D structure databases

ProteinModelPortaliP37941.
SMRiP37941. Positions 2-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP37941. 2 interactions.
STRINGi224308.BSU24040.

Proteomic databases

PaxDbiP37941.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14335; CAB14335; BSU24040.
GeneIDi938672.
KEGGibsu:BSU24040.
PATRICi18976636. VBIBacSub10457_2508.

Organism-specific databases

GenoListiBSU24040. [Micado]

Phylogenomic databases

eggNOGiCOG0022.
HOGENOMiHOG000281451.
InParanoidiP37941.
KOiK00167.
OMAiPIAEMQY.
OrthoDBiEOG6JQH4C.
PhylomeDBiP37941.

Enzyme and pathway databases

BioCyciBSUB:BSU24040-MONOMER.
MetaCyc:MONOMER-11684.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiODBB_BACSU
AccessioniPrimary (citable) accession number: P37941
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 7, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.