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P21882

- ODPB_BACSU

UniProt

P21882 - ODPB_BACSU

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
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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.
    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

    MAQMTMIQAI TDALRTELKN DENVLVFGED VGVNGGVFRA TEGLQKEFGE    50
    DRVFDTPLAE SGIGGLALGL GLNGFRPVME IQFFGFVYEV MDSVSGQMAR 100
    MRYRSGGRWT SPVTIRSPFG GGVHTPELHA DSLEGLVAQQ PGIKVVIPST 150
    PYDAKGLLIS AIRDNDPVVF LEHMKLYRSF RQEVPEEEYT IELGKADVKR 200
    EGTDLSIITY GAMVHESLKA ADELEKDGIS AEVVDLRTVS PLDIDTIIAS 250
    VEKTGRAIVV QEAQKQAGIA ANVVAEINDR AILSLEAPVL RVAAPDTVFP 300
    FSQAESVWLP NHKDVLETAR KVLEF 325
    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.
    WP_003232313.1. NZ_CM000487.1.

    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.
    WP_003232313.1. NZ_CM000487.1.

    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.
    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

    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 1, 2014
    This is version 107 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