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A5VSQ0

- ODO1_BRUO2

UniProt

A5VSQ0 - ODO1_BRUO2

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

Organism
Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (10 Jul 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).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

    BioCyciBOVI444178:GH2V-1849-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:sucAUniRule annotation
    Synonyms:odhAUniRule annotation
    Ordered Locus Names:BOV_1852
    OrganismiBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
    Taxonomic identifieri444178 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000006383: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 100410042-oxoglutarate dehydrogenase E1 componentPRO_1000065700Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi444178.BOV_1852.

    Structurei

    3D structure databases

    ProteinModelPortaliA5VSQ0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0567.
    HOGENOMiHOG000259586.
    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.

    A5VSQ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKQEQAPGR ANDVFALTSF LYGGNADYIE ELYAKYEDDP NSVDPQWRDF     50
    FAKLGDNADD VKKNAEGPSW TRKNWPIAAN GELVSALDGN WAEVEKHVTD 100
    KLKGKAAKGE AKGAAGTPLT AEEITQAARD SVRAIMMIRA YRMRGHLHAN 150
    LDPLGLAEKP NDYNELEPEN YGFTPADYNR KIFIDNVLGL EYATVPEMLD 200
    ILKRTYCGAI GVEFMHISDP AEKAWIQERI EGPDKKVAFT PEGKMAILSK 250
    LIEAEGFEQF IDVKYKGTKR FGLDGGESLI PALEQIVKRG GQMGLKEVVL 300
    GMAHRGRLNV LSQVMGKPHR AIFHEFKGGS YTPDDVEGSG DVKYHLGASS 350
    DREFDGNKVH LSLTANPSHL EIVNPVVMGK ARAKQDLLVG RTRDDMVPLS 400
    ERAKVLPLLL HGDAAFAGQG VVAECLGLSG LKGHRVAGTL HFIINNQIGF 450
    TTNPAFSRSS PYPSDVAKMI EAPIFHVNGD DPEAVVFAAK VATEFRMTFH 500
    KPVVIDMFCY RRFGHNEGDE PSFTQPLMYK AIRAHKTTVQ LYGEKLIAEG 550
    LVTQDDIDRM KADWRQKLEG EFEAGQSYKP NKADWLDGAW AGLRTADNAD 600
    EQRCGKTAVP VKTLKEIGKK LVEVPKDFHV HRTIQRFLDN RAKMMETGEG 650
    IDWATAESLA FGSLAVEGHP IRLSGQDVER GTFSQRHTVL YDQENQNRYI 700
    PLNNLQKGQA IYEAINSMLS EEAVLGYEYG YSLSDPRALV LWEAQFGDFA 750
    NGAQVVFDQF ISSGERKWLR MSGLVCLLPH GFEGQGPEHS SARLERYLQL 800
    CAEDNMQVAN VTTPANYFHI LRRQMKRDFR KPLIMMTPKS LLRHKRAIST 850
    LAELSGESSF HRLLWDDAQY NKDEGIKLQK DAKIRRVVLC SGKVYYDLYE 900
    EREKRGIDDV YLLRVEQLYP FPAKALINEL SRFRHAEMVW CQEEPKNMGA 950
    WSFIDPYLEW VLAHIDAKHQ RVRYAGRPAA ASPATGLMSK HLAQLAAFLE 1000
    DALG 1004
    Length:1,004
    Mass (Da):112,573
    Last modified:July 10, 2007 - v1
    Checksum:i4A5C3483F838816C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000708 Genomic DNA. Translation: ABQ60359.1.
    RefSeqiYP_001259747.1. NC_009505.1.

    Genome annotation databases

    EnsemblBacteriaiABQ60359; ABQ60359; BOV_1852.
    GeneIDi5201823.
    KEGGibov:BOV_1852.
    PATRICi17863809. VBIBruOvi136990_3279.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000708 Genomic DNA. Translation: ABQ60359.1 .
    RefSeqi YP_001259747.1. NC_009505.1.

    3D structure databases

    ProteinModelPortali A5VSQ0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 444178.BOV_1852.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ60359 ; ABQ60359 ; BOV_1852 .
    GeneIDi 5201823.
    KEGGi bov:BOV_1852.
    PATRICi 17863809. VBIBruOvi136990_3279.

    Phylogenomic databases

    eggNOGi COG0567.
    HOGENOMi HOG000259586.
    KOi K00164.
    OMAi GHQNANL.
    OrthoDBi EOG6V1M1F.

    Enzyme and pathway databases

    BioCyci BOVI444178:GH2V-1849-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. Paulsen I.
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25840 / 63/290 / NCTC 10512.

    Entry informationi

    Entry nameiODO1_BRUO2
    AccessioniPrimary (citable) accession number: A5VSQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 51 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