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P37941

- ODBB_BACSU

UniProt

P37941 - ODBB_BACSU

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Protein

2-oxoisovalerate dehydrogenase subunit beta

Gene

bfmBAB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

Thiamine pyrophosphate.

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.
OMAiDKHRCLA.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M97391 Genomic DNA. Translation: AAA22279.1 .
D84432 Genomic DNA. Translation: BAA12599.1 .
AL009126 Genomic DNA. Translation: CAB14335.1 .
PIRi D69593.
RefSeqi NP_390284.1. NC_000964.3.

3D structure databases

ProteinModelPortali P37941.
SMRi P37941. Positions 2-327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P37941. 2 interactions.
STRINGi 224308.BSU24040.

Proteomic databases

PaxDbi P37941.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14335 ; CAB14335 ; BSU24040 .
GeneIDi 938672.
KEGGi bsu:BSU24040.
PATRICi 18976636. VBIBacSub10457_2508.

Organism-specific databases

GenoListi BSU24040. [Micado ]

Phylogenomic databases

eggNOGi COG0022.
HOGENOMi HOG000281451.
InParanoidi P37941.
KOi K00167.
OMAi DKHRCLA.
OrthoDBi EOG6JQH4C.
PhylomeDBi P37941.

Enzyme and pathway databases

BioCyci BSUB:BSU24040-MONOMER.
MetaCyc:MONOMER-11684.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProi IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view ]
Pfami PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 103 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