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Q65IH4

- ODO1_BACLD

UniProt

Q65IH4 - ODO1_BACLD

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Bacillus licheniformis (strain DSM 13 / ATCC 14580)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (25 Oct 2004)
      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

    BioCyciBLIC279010:GJ2P-2245-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:BLi02260, BL01452
    OrganismiBacillus licheniformis (strain DSM 13 / ATCC 14580)
    Taxonomic identifieri279010 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000000606: Chromosome, UP000000608: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9449442-oxoglutarate dehydrogenase E1 componentPRO_0000162167Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi279010.BL01452.

    Structurei

    3D structure databases

    ProteinModelPortaliQ65IH4.
    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.

    Q65IH4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFQNSMKQRM TWEEFHGPNL GYVLELYDQY VKDPESLDAD LKEMFDELGA    50
    PPGDIRAASQ KNEEADFTAG SIQKIASAVK LAEDIRTYGH LNASVNPLRK 100
    TQEKQELFPL AEYGLTEQDV KKIPASVICK DAPKEVTNGL EAIQYLRNTY 150
    KKSISFEFDH VHIFEERNWL MKKIESGELF TPKSKEKLVE VLRRLTEVES 200
    LEQFLHKTFV GQKRFSIEGL DALVPMLDDI IAKSVSAGTT NVNIGMAHRG 250
    RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSTGINYG WTGDVKYHLG 300
    ANRQIQDEHT KTARIALANN PSHLEFIDPI VEGSTRAAQE TRTESGYPVQ 350
    DVKKSMAILI HGDAAFPGEG IVAETLNLSQ LKGYQVGGAI HIIANNMIGF 400
    TTESNESRST KYASDLAKGF EIPIVHVNAD DPEACLSAVQ LAVEYRMTFN 450
    KDFLIDLIGY RRFGHNEMDE PSATQPMLYD AVRKHPTVKN IFAEKLIHKG 500
    IVDKETVGKI KDAVQKRLEE AYRKVPAKKE DMTHEIVLPE PVSNGFPDVD 550
    TSVDFETLRK INQELVSWPE NFNVFDKLKR ILERRAKAFE DDRKVDWSLA 600
    EAMAFASILK DGTPLRLTGQ DSERGTFAHR NLVLHDSKTG DEFIALHHLA 650
    DTKASFAVHN SPLSEGSVLG FEYGYNVSSP ETMVIWEAQF GDFANAAQVY 700
    FDQFISAGRA KWGQKSGLVV LLPHGYEGQG PEHSSGRTER FLQLAAENNW 750
    TVANLTSAAQ YFHILRRQAK MLLREEIRPL IIMTPKSLLR NPNTVSEVQE 800
    LSNSSFKPVY EMSGLSHQYD KVTRLVLSSG KVSIDISDHF NKMEGEKDWL 850
    HIARVEELYP FPAKHIKAIF SKLPNLEEIV WVQEEPQNMG AWNYIEPYLR 900
    EVAPKDVKVR YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN 944
    Length:944
    Mass (Da):106,671
    Last modified:October 25, 2004 - v1
    Checksum:i9E63C701C8847E39
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017333 Genomic DNA. Translation: AAU41140.1.
    CP000002 Genomic DNA. Translation: AAU23783.1.
    RefSeqiYP_006713619.1. NC_006322.1.
    YP_079421.1. NC_006270.3.

    Genome annotation databases

    EnsemblBacteriaiAAU23783; AAU23783; BL01452.
    AAU41140; AAU41140; BLi02260.
    GeneIDi3028258.
    3100388.
    KEGGibld:BLi02260.
    bli:BL01452.
    PATRICi18950158. VBIBacLic203714_2281.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017333 Genomic DNA. Translation: AAU41140.1 .
    CP000002 Genomic DNA. Translation: AAU23783.1 .
    RefSeqi YP_006713619.1. NC_006322.1.
    YP_079421.1. NC_006270.3.

    3D structure databases

    ProteinModelPortali Q65IH4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 279010.BL01452.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAU23783 ; AAU23783 ; BL01452 .
    AAU41140 ; AAU41140 ; BLi02260 .
    GeneIDi 3028258.
    3100388.
    KEGGi bld:BLi02260.
    bli:BL01452.
    PATRICi 18950158. VBIBacLic203714_2281.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BLIC279010:GJ2P-2245-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. "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
      Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
      J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 13 / ATCC 14580.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 13 / ATCC 14580.

    Entry informationi

    Entry nameiODO1_BACLD
    AccessioniPrimary (citable) accession number: Q65IH4
    Secondary accession number(s): Q62TX6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: October 25, 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3