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P65635

- ODP2_STAAM

UniProt

P65635 - ODP2_STAAM

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      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).

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei401 – 4011Sequence 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

    BioCyciSAUR158878:GJJ5-1114-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
    Gene namesi
    Name:pdhC
    Ordered Locus Names:SAV1095
    OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
    Taxonomic identifieri158878 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000002481: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162288Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N6-lipoyllysineBy similarity

    Proteomic databases

    PRIDEiP65635.

    2D gel databases

    World-2DPAGE0002:P65635.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

    Protein-protein interaction databases

    STRINGi158878.SAV1095.

    Structurei

    3D structure databases

    ProteinModelPortaliP65635.
    SMRiP65635. Positions 2-79, 126-160, 187-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7676Lipoyl-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.
    PhylomeDBiP65635.

    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.

    P65635-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFEFRLPDI GEGIHEGEIV KWFVKAGDTI EEDDVLAEVQ NDKSVVEIPS    50
    PVSGTVEEVM VEEGTVAVVG DVIVKIDAPD AEDMQFKGHD DDSSSKEEPA 100
    KEEAPAEQAP VATQTEEVDE NRTVKAMPSV RKYAREKGVN IKAVSGSGKN 150
    GRITKEDVDA YLNGGAPTAS NESAASATSE EVAETPAAPA AVSLEGDFPE 200
    TTEKIPAMRR AIAKAMVNSK HTAPHVTLMD EIDVQALWDH RKKFKEIAAE 250
    QGTKLTFLPY VVKALVSALK KYPALNTSFN EEAGEIVHKH YWNIGIAADT 300
    DRGLLVPVVK HADRKSIFQI SDEINELAVK ARDGKLTADE MKGATCTISN 350
    IGSAGGQWFT PVINHPEVAI LGIGRIAQKP IVKDGEIVAA PVLALSLSFD 400
    HRQIDGATGQ NAMNHIKRLL NNPELLLMEG 430
    Length:430
    Mass (Da):46,368
    Last modified:October 11, 2004 - v1
    Checksum:i4050074CAE5ACDA4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB57257.1.
    RefSeqiNP_371619.1. NC_002758.2.

    Genome annotation databases

    EnsemblBacteriaiBAB57257; BAB57257; SAV1095.
    GeneIDi1121072.
    KEGGisav:SAV1095.
    PATRICi19562889. VBIStaAur52173_1123.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB57257.1 .
    RefSeqi NP_371619.1. NC_002758.2.

    3D structure databases

    ProteinModelPortali P65635.
    SMRi P65635. Positions 2-79, 126-160, 187-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158878.SAV1095.

    2D gel databases

    World-2DPAGE 0002:P65635.

    Proteomic databases

    PRIDEi P65635.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB57257 ; BAB57257 ; SAV1095 .
    GeneIDi 1121072.
    KEGGi sav:SAV1095.
    PATRICi 19562889. VBIStaAur52173_1123.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281564.
    KOi K00627.
    OMAi EPLKGFH.
    OrthoDBi EOG610413.
    PhylomeDBi P65635.

    Enzyme and pathway databases

    BioCyci SAUR158878:GJJ5-1114-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Mu50 / ATCC 700699.

    Entry informationi

    Entry nameiODP2_STAAM
    AccessioniPrimary (citable) accession number: P65635
    Secondary accession number(s): Q99V06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 69 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3