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P21882

- ODPB_BACSU

UniProt

P21882 - ODPB_BACSU

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Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
The B.subtilis PDH complex possesses also branched-chain 2-oxoacid dehydrogenase (BCDH) activity.

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Thiamine pyrophosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphateBy similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciBSUB:BSU14590-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta (EC:1.2.4.1)
Alternative name(s):
S complex, 36 kDa subunit
Gene namesi
Name:pdhB
Synonyms:aceB
Ordered Locus Names:BSU14590
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU14590. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 325324Pyruvate dehydrogenase E1 component subunit betaPRO_0000162222Add
BLAST

Proteomic databases

PaxDbiP21882.

PTM databases

PhosSiteiP0802226.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

IntActiP21882. 1 interaction.
MINTiMINT-8365509.
STRINGi224308.BSU14590.

Structurei

3D structure databases

ProteinModelPortaliP21882.
SMRiP21882. Positions 2-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0022.
HOGENOMiHOG000281451.
InParanoidiP21882.
KOiK00162.
OMAiWSKHELG.
OrthoDBiEOG6JQH4C.
PhylomeDBiP21882.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21882-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQMTMIQAI TDALRTELKN DENVLVFGED VGVNGGVFRA TEGLQKEFGE
60 70 80 90 100
DRVFDTPLAE SGIGGLALGL GLNGFRPVME IQFFGFVYEV MDSVSGQMAR
110 120 130 140 150
MRYRSGGRWT SPVTIRSPFG GGVHTPELHA DSLEGLVAQQ PGIKVVIPST
160 170 180 190 200
PYDAKGLLIS AIRDNDPVVF LEHMKLYRSF RQEVPEEEYT IELGKADVKR
210 220 230 240 250
EGTDLSIITY GAMVHESLKA ADELEKDGIS AEVVDLRTVS PLDIDTIIAS
260 270 280 290 300
VEKTGRAIVV QEAQKQAGIA ANVVAEINDR AILSLEAPVL RVAAPDTVFP
310 320
FSQAESVWLP NHKDVLETAR KVLEF
Length:325
Mass (Da):35,474
Last modified:January 23, 2007 - v2
Checksum:i887EECA29C0C4E25
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M57435 Genomic DNA. Translation: AAA62682.1.
AF012285 Genomic DNA. Translation: AAC24933.1.
AL009126 Genomic DNA. Translation: CAB13332.1.
PIRiC36718.
RefSeqiNP_389342.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13332; CAB13332; BSU14590.
GeneIDi939496.
KEGGibsu:BSU14590.
PATRICi18974711. VBIBacSub10457_1547.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M57435 Genomic DNA. Translation: AAA62682.1 .
AF012285 Genomic DNA. Translation: AAC24933.1 .
AL009126 Genomic DNA. Translation: CAB13332.1 .
PIRi C36718.
RefSeqi NP_389342.1. NC_000964.3.

3D structure databases

ProteinModelPortali P21882.
SMRi P21882. Positions 2-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P21882. 1 interaction.
MINTi MINT-8365509.
STRINGi 224308.BSU14590.

PTM databases

PhosSitei P0802226.

Proteomic databases

PaxDbi P21882.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13332 ; CAB13332 ; BSU14590 .
GeneIDi 939496.
KEGGi bsu:BSU14590.
PATRICi 18974711. VBIBacSub10457_1547.

Organism-specific databases

GenoListi BSU14590. [Micado ]

Phylogenomic databases

eggNOGi COG0022.
HOGENOMi HOG000281451.
InParanoidi P21882.
KOi K00162.
OMAi WSKHELG.
OrthoDBi EOG6JQH4C.
PhylomeDBi P21882.

Enzyme and pathway databases

BioCyci BSUB:BSU14590-MONOMER.

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. "Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase."
    Hemilae H.O., Palva A., Paulin L., Arvidson S., Palva I.
    J. Bacteriol. 172:5052-5063(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis 168 chromosome: sequencing of a 27 kb segment and identification of several genes in the area."
    Winters P., Caldwell R.M., Enfield L., Ferrari E.
    Microbiology 142:3033-3037(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "Sequence analysis of the mobA-ampS region of the Bacillus subtilis chromosome."
    Caldwell R.M., Ferrari E.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  4. "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 nameiODPB_BACSU
AccessioniPrimary (citable) accession number: P21882
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3