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Q99U74

- ODO1_STAAN

UniProt

Q99U74 - ODO1_STAAN

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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).UniRule annotation

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.UniRule annotation

    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

    BioCyciSAUR158879:GJCB-1312-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-oxoglutarate dehydrogenase E1 componentUniRule annotation (EC:1.2.4.2UniRule annotation)
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenaseUniRule annotation
    Gene namesi
    Name:odhAUniRule annotation
    Ordered Locus Names:SA1245
    OrganismiStaphylococcus aureus (strain N315)
    Taxonomic identifieri158879 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000751: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9109102-oxoglutarate dehydrogenase E1 componentPRO_0000162178Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi158879.SA1245.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99U74.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0567.
    HOGENOMiHOG000259588.
    KOiK00164.
    OMAiGFTTAPH.
    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.

    Q99U74-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKRV    50
    MRLIDNIRQY GHLKADIYPV NPPKRKHVPK LEIEDFDLDQ QTLEGISAGI 100
    VSDHFADIYD NAYEAILRME KRYKGPIAFE YTHINNNTER GWLKRRIETP 150
    YKVTLNNNEK RALFKQLAYV EGFEKYLHKN FVGAKRFSIE GVDALVPMLQ 200
    RTITIAAKEG IKNIQIGMAH RGRLNVLTHV LEKPYEMMIS EFMHTDPMKF 250
    LPEDGSLQLT AGWTGDVKYH LGGIKTTDSY GTMQRIALAN NPSHLEIVAP 300
    VVEGRTRAAQ DDTQRAGAPT TDHHKAMPII IHGDAAYPGQ GINFETMNLG 350
    NLKGYSTGGS LHIITNNRIG FTTEPIDARS TTYSTDVAKG YDVPIFHVNA 400
    DDVEATIEAI DIAMEFRKEF HKDVVIDLVG YRRFGHNEMD EPSITNPVPY 450
    QNIRKHDSVE YVFGKKLVNE GVISEDEMHS FIEQVQKELR QAHDKINKAD 500
    KMDNPDMEKP AELALPLQAD EQSFTFDHLK EINDALLTYP DGFNILKKLN 550
    KVLEKRHEPF NKEDGLVDWA QAEQLAFATI LQDGTPIRLT GQDSERGTFS 600
    HRHAVLHDEQ TGETYTPLHH VPDQKATFDI HNSPLSEAAV VGFEYGYNVE 650
    NKKSFNIWEA QYGDFANMSQ MIFDNFLFSS RSKWGERSGL TLFLPHAYEG 700
    QGPEHSSARL ERFLQLAAEN NCTVVNLSSS SNYFHLLRAQ AASLDSEQMR 750
    PLVVMSPKSL LRNKTVAKPI DEFTSGGFEP ILTESYQADK VTKVILATGK 800
    MFIDLKEALA KNPDESVLLV AIERLYPFPE EEIEALLAQL PKLEEVSWVQ 850
    EEPKNQGAWL YVYPYVKVLV ADKYDLSYHG RIQRAAPAEG DGEIHKLVQN 900
    KIIENALKNN 910
    Length:910
    Mass (Da):103,112
    Last modified:June 1, 2001 - v1
    Checksum:i7803AAED537CF247
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42505.1.
    PIRiE89918.
    RefSeqiNP_374526.1. NC_002745.2.
    WP_000180688.1. NC_002745.2.

    Genome annotation databases

    EnsemblBacteriaiBAB42505; BAB42505; BAB42505.
    GeneIDi1124084.
    KEGGisau:SA1245.
    PATRICi19574740. VBIStaAur116463_1339.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB42505.1 .
    PIRi E89918.
    RefSeqi NP_374526.1. NC_002745.2.
    WP_000180688.1. NC_002745.2.

    3D structure databases

    ProteinModelPortali Q99U74.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158879.SA1245.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB42505 ; BAB42505 ; BAB42505 .
    GeneIDi 1124084.
    KEGGi sau:SA1245.
    PATRICi 19574740. VBIStaAur116463_1339.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SAUR158879:GJCB-1312-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: N315.
    2. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
      Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
      Submitted (OCT-2007) to UniProtKB
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: N315.

    Entry informationi

    Entry nameiODO1_STAAN
    AccessioniPrimary (citable) accession number: Q99U74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 77 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