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A7X295

- ODO1_STAA1

UniProt

A7X295 - ODO1_STAA1

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (23 Oct 2007)
      Previous versions | rss
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    Functioni

    The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.By similarity

    Catalytic activityi

    2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

    Cofactori

    Thiamine pyrophosphate.By similarity

    GO - Molecular functioni

    1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-EC
    2. thiamine pyrophosphate binding Source: InterPro

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW
    2. tricarboxylic acid cycle Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciSAUR418127:GJP9-1419-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenase
    Gene namesi
    Name:odhA
    Ordered Locus Names:SAHV_1401
    OrganismiStaphylococcus aureus (strain Mu3 / ATCC 700698)
    Taxonomic identifieri418127 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000001130: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9329322-oxoglutarate dehydrogenase E1 componentPRO_0000313016Add
    BLAST

    Proteomic databases

    PRIDEiA7X295.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi418127.SAHV_1401.

    Structurei

    3D structure databases

    ProteinModelPortaliA7X295.
    SMRiA7X295. Positions 71-929.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0567.
    HOGENOMiHOG000259588.
    KOiK00164.
    OMAiGHQNANL.
    OrthoDBiEOG6V1M1F.

    Family and domain databases

    Gene3Di3.40.50.970. 2 hits.
    HAMAPiMF_01169. SucA_OdhA.
    InterProiIPR011603. 2oxoglutarate_DH_E1.
    IPR023784. 2oxoglutarate_DH_E1_bac.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view]
    PANTHERiPTHR23152. PTHR23152. 1 hit.
    PfamiPF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 2 hits.
    TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A7X295-1 [UniParc]FASTAAdd to Basket

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    MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKND    50
    DSIVPALKST SSQNSDGTIK RVMRLIDNIR QYGHLKADIY PVNPPKRKHV 100
    PKLEIEDFDL DQQTLEGISA GIVSDHFADI YDNAYEAILR MEKRYKGPIA 150
    FEYTHINNNT ERGWLKRRIE TPYKVTLNNN EKRALFKQLA YVEGFEKYLH 200
    KNFVGAKRFS IEGVDALVPM LQRTITIAAK EGIKNIQIGM AHRGRLNVLT 250
    HVLEKPYEMM ISEFMHTDPM KFLPEDGSLQ LTAGWTGDVK YHLGGIKTTD 300
    SYGTMQRIAL ANNPSHLEIV APVVEGRTRA AQDDTQRAGA PTTDHHKAMP 350
    IIIHGDAAYP GQGINFETMN LGNLKGYSTG GSLHIITNNR IGFTTEPIDA 400
    RSTTYSTDVA KGYDVPIFHV NADDVEATIE AIDIAMEFRK EFHKDVVIDL 450
    VGYRRFGHNE MDEPSITNPV PYQNIRKHDS VEYVFGKKLV NEGVISEDEM 500
    HSFIEQVQKE LRQAHDKINK ADKMDNPDME KPAELALPLQ ADEQSFTFDH 550
    LKEINDALLT YPDGFNILKK LNKVLEKRHE PFNKEDGLVD WAQAEQLAFA 600
    TILQDGTPIR LTGQDSERGT FSHRHAVLHD EQTGETYTPL HHVPDQKATF 650
    DIHNSPLSEA AVVGFEYGYN VENKKSFNIW EAQYGDFANM SQMIFDNFLF 700
    SSRSKWGERS GLTLFLPHAY EGQGPEHSSA RLERFLQLAA ENNCTVVNLS 750
    SSSNYFHLLR AQAASLDSEQ MRPLVVMSPK SLLRNKTVAK PIDEFTSGGF 800
    EPILTESYQA DKVTKVILAT GKMFIDLKEA LAKNPDESVL LVAIERLYPF 850
    PEEEIEALLA QLPNLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY 900
    HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN 932
    Length:932
    Mass (Da):105,357
    Last modified:October 23, 2007 - v1
    Checksum:iF671CE1A65ADAF6D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461T → I in CAD92197. 1 PublicationCurated
    Sequence conflicti864 – 8641N → K in CAD92197. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ564530 Genomic DNA. Translation: CAD92197.1.
    AP009324 Genomic DNA. Translation: BAF78284.1.
    RefSeqiYP_001441991.1. NC_009782.1.

    Genome annotation databases

    EnsemblBacteriaiBAF78284; BAF78284; SAHV_1401.
    GeneIDi5561127.
    KEGGisaw:SAHV_1401.
    PATRICi19557834. VBIStaAur127830_1434.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ564530 Genomic DNA. Translation: CAD92197.1 .
    AP009324 Genomic DNA. Translation: BAF78284.1 .
    RefSeqi YP_001441991.1. NC_009782.1.

    3D structure databases

    ProteinModelPortali A7X295.
    SMRi A7X295. Positions 71-929.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 418127.SAHV_1401.

    Proteomic databases

    PRIDEi A7X295.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAF78284 ; BAF78284 ; SAHV_1401 .
    GeneIDi 5561127.
    KEGGi saw:SAHV_1401.
    PATRICi 19557834. VBIStaAur127830_1434.

    Phylogenomic databases

    eggNOGi COG0567.
    HOGENOMi HOG000259588.
    KOi K00164.
    OMAi GHQNANL.
    OrthoDBi EOG6V1M1F.

    Enzyme and pathway databases

    BioCyci SAUR418127:GJP9-1419-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.970. 2 hits.
    HAMAPi MF_01169. SucA_OdhA.
    InterProi IPR011603. 2oxoglutarate_DH_E1.
    IPR023784. 2oxoglutarate_DH_E1_bac.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view ]
    PANTHERi PTHR23152. PTHR23152. 1 hit.
    Pfami PF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 2 hits.
    TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genetic analysis of seventeen genes in Staphylococcus aureus with reduced susceptibility to vancomycin (VRSA) and hetero-VRSA (hVRSA)."
      Wootton M., Avison M.B., Bennett P.M., Howe R.A., MacGowan A.P., Walsh T.R.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance."
      Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.
      Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Mu3 / ATCC 700698.

    Entry informationi

    Entry nameiODO1_STAA1
    AccessioniPrimary (citable) accession number: A7X295
    Secondary accession number(s): Q7ASB7
    , Q7WRM3, Q7WRN1, Q7WRX0, Q7WZ40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 48 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