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P21883

- ODP2_BACSU

UniProt

P21883 - ODP2_BACSU

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (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

    Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei413 – 4131Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Glycolysis

    Enzyme and pathway databases

    BioCyciBSUB:BSU14600-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:2.3.1.12)
    Alternative name(s):
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
    E2
    S complex, 48 kDa subunit
    Gene namesi
    Name:pdhC
    Synonyms:aceC
    Ordered Locus Names:BSU14600
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU14600. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 442441Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162274Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N6-lipoyllysine1 Publication

    Proteomic databases

    PaxDbiP21883.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Protein-protein interaction databases

    IntActiP21883. 1 interaction.
    STRINGi224308.BSU14600.

    Structurei

    3D structure databases

    ProteinModelPortaliP21883.
    SMRiP21883. Positions 2-81, 139-176, 197-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7675Lipoyl-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni140 – 18243E1/E3 bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281564.
    KOiK00627.
    OMAiEPLKGFH.
    OrthoDBiEOG610413.
    PhylomeDBiP21883.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P21883-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFEFKLPDI GEGIHEGEIV KWFVKPNDEV DEDDVLAEVQ NDKAVVEIPS    50
    PVKGKVLELK VEEGTVATVG QTIITFDAPG YEDLQFKGSD ESDDAKTEAQ 100
    VQSTAEAGQD VAKEEQAQEP AKATGAGQQD QAEVDPNKRV IAMPSVRKYA 150
    REKGVDIRKV TGSGNNGRVV KEDIDSFVNG GAQEAAPQET AAPQETAAKP 200
    AAAPAPEGEF PETREKMSGI RKAIAKAMVN SKHTAPHVTL MDEVDVTNLV 250
    AHRKQFKQVA ADQGIKLTYL PYVVKALTSA LKKFPVLNTS IDDKTDEVIQ 300
    KHYFNIGIAA DTEKGLLVPV VKNADRKSVF EISDEINGLA TKAREGKLAP 350
    AEMKGASCTI TNIGSAGGQW FTPVINHPEV AILGIGRIAE KAIVRDGEIV 400
    AAPVLALSLS FDHRMIDGAT AQNALNHIKR LLNDPQLILM EA 442
    Length:442
    Mass (Da):47,539
    Last modified:January 23, 2007 - v2
    Checksum:i73AFC68220717C34
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57435 Genomic DNA. Translation: AAA62683.1.
    AF012285 Genomic DNA. Translation: AAC24934.1.
    AL009126 Genomic DNA. Translation: CAB13333.1.
    PIRiD36718.
    RefSeqiNP_389343.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13333; CAB13333; BSU14600.
    GeneIDi936010.
    KEGGibsu:BSU14600.
    PATRICi18974713. VBIBacSub10457_1548.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57435 Genomic DNA. Translation: AAA62683.1 .
    AF012285 Genomic DNA. Translation: AAC24934.1 .
    AL009126 Genomic DNA. Translation: CAB13333.1 .
    PIRi D36718.
    RefSeqi NP_389343.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P21883.
    SMRi P21883. Positions 2-81, 139-176, 197-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P21883. 1 interaction.
    STRINGi 224308.BSU14600.

    Proteomic databases

    PaxDbi P21883.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13333 ; CAB13333 ; BSU14600 .
    GeneIDi 936010.
    KEGGi bsu:BSU14600.
    PATRICi 18974713. VBIBacSub10457_1548.

    Organism-specific databases

    GenoListi BSU14600. [Micado ]

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281564.
    KOi K00627.
    OMAi EPLKGFH.
    OrthoDBi EOG610413.
    PhylomeDBi P21883.

    Enzyme and pathway databases

    BioCyci BSUB:BSU14600-MONOMER.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    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], LIPOYLATION AT LYS-43.
      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 nameiODP2_BACSU
    AccessioniPrimary (citable) accession number: P21883
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 110 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
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3