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Q4L6C4

- ODO1_STAHJ

UniProt

Q4L6C4 - ODO1_STAHJ

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (02 Aug 2005)
      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

    BioCyciSHAE279808:GJX7-1546-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:SH1492
    OrganismiStaphylococcus haemolyticus (strain JCSC1435)
    Taxonomic identifieri279808 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000543: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9349342-oxoglutarate dehydrogenase E1 componentPRO_0000162184Add
    BLAST

    Proteomic databases

    PRIDEiQ4L6C4.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi279808.SH1492.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4L6C4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

    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.

    Q4L6C4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKDNKDVTE APVNFGANLG LMLDLYDDYL QDPSSVPDDL QVLFSTIKNG    50
    EAHVAAKSTT EGSGSSAGDG TIKRIMRLID NIRQYGHLKA DIYPVNAPKR 100
    TNLPKLEIEE FNLDKETLEN VSAEIVSDHF KDIYDNAYEA IERMEKRYKG 150
    PIAFEYNHIN NNKERTWLKR RIETPYRANI NNDERKKLFD TLAHVEGFEK 200
    YLHKNFVGAK RFSIEGVDTL VPMLQHTLKR AAEIEINNIQ IGMAHRGRLN 250
    VLTHVLEKPY EMMISEFMHT DPMKFLPEDG SLELTAGWTG DVKYHLGGVK 300
    TTSSYGIEQR ISLANNPSHL EIVAPVVIGK TRASQDDTKH AGKPTTDFHK 350
    GMPIIIHGDA AYPGQGINFE TMNLSNLDGY STGGALHIIT NNRIGFTTEP 400
    VDGRSTTYST DIAKGYDVPI LHVNADDVEA TIEAIDIAME FRKEFHKDFV 450
    IDLVGYRRYG HNEMDEPSIT NPLPYHNIRK HDSVEIIYGN KLVEDGVISK 500
    EQMEDVMDKV QKEMRAAQDK IDKSDKMDNP DMERPESLQE PLQSDDKDFS 550
    VDHLKEINDA MLTYPEDFHV LKKLNKVLEK RREPFESENG LVDWAQAEQL 600
    AFATIVQDGI SVRLTGQDSE RGTFSHRHAV LHDEENGDTF TPLHHVPNQK 650
    ATFEVHNSPL SEAAVVGFEY GYNVENKNSM NIWEAQYGDF SNMAQMMFDN 700
    FMSSARAKWG ERSGLTLFLP HAFEGQGPEH SSARLERFLQ LAAENNSTVV 750
    NLSSSSNYFH LLRAQAKSLG TEAMRPLIVM SPKSLLRNKT VAKPIDQFTS 800
    GGFKPIIVED GNKEKVTKLV LASGKMFIDL KEHLAKNPDD SILLVAVDRL 850
    YPFPEGEIKE VLNELPNLET VSWVQEEPKN QGAWLFVYPY LKSLVGNQFN 900
    LSYHGRIQRA APAEGDGEIH KLVQNQIIES SIEK 934
    Length:934
    Mass (Da):105,479
    Last modified:August 2, 2005 - v1
    Checksum:i7D9E801A49E880E9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006716 Genomic DNA. Translation: BAE04801.1.
    RefSeqiYP_253407.1. NC_007168.1.

    Genome annotation databases

    EnsemblBacteriaiBAE04801; BAE04801; SH1492.
    GeneIDi3481998.
    KEGGisha:SH1492.
    PATRICi19619095. VBIStaHae67511_1471.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006716 Genomic DNA. Translation: BAE04801.1 .
    RefSeqi YP_253407.1. NC_007168.1.

    3D structure databases

    ProteinModelPortali Q4L6C4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 279808.SH1492.

    Proteomic databases

    PRIDEi Q4L6C4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAE04801 ; BAE04801 ; SH1492 .
    GeneIDi 3481998.
    KEGGi sha:SH1492.
    PATRICi 19619095. VBIStaHae67511_1471.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SHAE279808:GJX7-1546-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. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
      Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
      J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JCSC1435.

    Entry informationi

    Entry nameiODO1_STAHJ
    AccessioniPrimary (citable) accession number: Q4L6C4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: August 2, 2005
    Last modified: October 1, 2014
    This is version 66 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