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Q73BN8

- ODO1_BACC1

UniProt

Q73BN8 - ODO1_BACC1

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (05 Jul 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

    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:BCE_1380
    OrganismiBacillus cereus (strain ATCC 10987)
    Taxonomic identifieri222523 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000002527: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9559552-oxoglutarate dehydrogenase E1 componentPRO_0000162162Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi222523.BCE_1380.

    Structurei

    3D structure databases

    ProteinModelPortaliQ73BN8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0567.
    HOGENOMiHOG000259588.
    KOiK00164.
    OMAiQHAPNKE.
    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.

    Q73BN8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRKNTTTNP WAKFHGPNLG YVIEQYDLYV TGAGSVDPEL QELFEIFGAP    50
    SFQDDVVTGD NTATHFSPQN TGNIEKILKV VQLVEQIRSF GHTLAHINPM 100
    EDAANGQSLL EKAMNELSDA DLKAIPAKTV WQDAPEGIHT ALDVIHRLKE 150
    VYTQTLAYEF SHIQDSEERA WLHQMVESNS LRQPLSNKKR TALLKRLTAV 200
    EGFEQFLHKT FVGQKRFSIE GVDMLVPVLD EIVLEGAKNG VEDVMIGMAH 250
    RGRLSVLAHV LEKPYSHMFA EFKHAKIEGA VANSGWTGDV KYHLGREQVV 300
    SNEEVSTRVT LANNPSHLEF VNPVVEGFAR AAQENRKKSG LPEQDTSKSF 350
    VILVHGDAAF PGQGIVSETL NLSRLNAYQT GGTIHVIANN AVGFTTDSYD 400
    SRSTKYSSDL AKGFDIPIVH VNADDPEACL AAANLAIQYR MLFKKDFLID 450
    LIGYRRYGHN EMDDPAVTQP QVYKKIKNHP TVRAIYADQL QAAGVLNADE 500
    IETITQFIQE QLKSDYAQVP PADTSDATIH VKVPDVVAKG IQPIDTGVEL 550
    DSLRAINEGL LSWPEGFNVY PKVKKILERR KDALEENGKI EWALAESLAF 600
    ASILQEGTPI RLTGQDSQRG TFAHRHIVLH DTDTNETYSP LHRLPNINAS 650
    FSVHNSPLSE AAVVGYEYGY NVFAPETLVM WEAQYGDFSN TAQALFDQYV 700
    SAGRAKWGQK SGLVLLLPHG YEGQGPEHSS ARPERFLQLA AENNWTVANL 750
    TSAAQYFHIL RRQASVLGTE AVRPLVLMTP KSLLRHPLTL STASQLSEGR 800
    FQPALEQENL GTKPNKVKRL VLSTGKMAID LAAEIESGKH EYNLDEIHIV 850
    RIEQLYPFPA EKVQSIIKRF KNLEEIIWVQ EEPRNMGAWH YMAPILFELA 900
    GDKVKTGYIG RPDRSSPSGG DPFAHKAEQE LIVAHALDVK YNFRQDKLEI 950
    EVFSN 955
    Length:955
    Mass (Da):106,460
    Last modified:July 5, 2004 - v1
    Checksum:i4C2186C7E77968EA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS40309.1.
    RefSeqiNP_977701.1. NC_003909.8.
    WP_000197151.1. NC_003909.8.

    Genome annotation databases

    EnsemblBacteriaiAAS40309; AAS40309; BCE_1380.
    GeneIDi2748048.
    KEGGibca:BCE_1380.
    PATRICi18851616. VBIBacCer118379_1313.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS40309.1 .
    RefSeqi NP_977701.1. NC_003909.8.
    WP_000197151.1. NC_003909.8.

    3D structure databases

    ProteinModelPortali Q73BN8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 222523.BCE_1380.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS40309 ; AAS40309 ; BCE_1380 .
    GeneIDi 2748048.
    KEGGi bca:BCE_1380.
    PATRICi 18851616. VBIBacCer118379_1313.

    Phylogenomic databases

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

    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 genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
      Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
      Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10987.

    Entry informationi

    Entry nameiODO1_BACC1
    AccessioniPrimary (citable) accession number: Q73BN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 71 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