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C5D802

- ODO1_GEOSW

UniProt

C5D802 - ODO1_GEOSW

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Geobacillus sp. (strain WCH70)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      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

    BioCyciGSP471223:GH2C-1003-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:GWCH70_0919
    OrganismiGeobacillus sp. (strain WCH70)
    Taxonomic identifieri471223 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
    ProteomesiUP000002386: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9529522-oxoglutarate dehydrogenase E1 componentPRO_1000213736Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi471223.GWCH70_0919.

    Structurei

    3D structure databases

    ProteinModelPortaliC5D802.
    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.

    C5D802-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKQTMNYAE PWSQFYGPNL GYVMEMYEQY LEDPDSVDPE LKQLFKEWGA    50
    PTTEAERFDH SESAAKTYQT FRLPENPTIF SKLVAAVKLA DKIRHYGHLA 100
    ADINPLNTQN KDTRRIELSE FDLTEDDLKQ IPVAFICPHA PAHVKNGLDA 150
    INHLRKIYTD KIAFEFSQVH NLEERNWLIS QIESGAYYPS LTNEEKVALL 200
    RRLTEVEGFE KFLHRTFVGQ KRFSIEGLDS MVPLLDELIR HSIEEEVKAV 250
    NIGMAHRGRL NVLAHVLGKP YEMIFAEFQH AESKDFMPSE GSVAITYGWT 300
    GDVKYHLGAA RRLRNKNEHT MRITLANNPS HLEVVNPVVL GFTRAAQEDR 350
    SNAGVPSQDT DSAFAIMIHG DAAFPGQGIV AETLNLSRLQ GYQTGGSIHI 400
    IANNMIGFTT ESYDSRSTKY ASDIAKGFEI PIVHVNADDP EACLAAANLA 450
    FAYRKRFKKD FVIDLIGYRR FGHNEMDEPM ATNPTMYSII QQHPTVRQLY 500
    AQKLIEKGII TKEAVEEMER EVAERLKIAY EKVPKDESKL DFIMDPPKPV 550
    ASKLPFVKTS VEKDVLRRLN KELLQFPSDF HVFNKLERIL KRREGVFDGK 600
    GKIDWAHAEI LAFATILRDG VPIRLTGQDS QRGTFAQRHL VLHDMKTGEE 650
    FVPLHHISDA NASFVVYNSP LTEAAVLGYE YGYNVFAPET LVLWEAQFGD 700
    FANMAQVMFD QFISSGRAKW GQKSGLVMLL PHGYEGQGPE HSSGRLERFL 750
    QLAAENNWTV ANLSTAAQYF HILRRQAGIL QREEVRPLVL MTPKSLLRHP 800
    LAASDVEEFT NGQFHPVIEQ KGLGENREKV ERIILCTGKF AIDLAEQINK 850
    MEGLDWLHIV RVEELYPFPK EELQAIFARY PNVKEIIWAQ EEPKNMGSWC 900
    YVEPKLREIA PDEVDVSYIG RRRRASPAEG DPVVHRKEQE RIIQCALTKK 950
    EQ 952
    Length:952
    Mass (Da):108,481
    Last modified:July 28, 2009 - v1
    Checksum:iD00671DCFA511D3B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001638 Genomic DNA. Translation: ACS23783.1.
    RefSeqiWP_015863262.1. NC_012793.1.
    YP_002949049.1. NC_012793.1.

    Genome annotation databases

    EnsemblBacteriaiACS23783; ACS23783; GWCH70_0919.
    GeneIDi7976647.
    KEGGigwc:GWCH70_0919.
    PATRICi21970752. VBIGeoSp101709_0991.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001638 Genomic DNA. Translation: ACS23783.1 .
    RefSeqi WP_015863262.1. NC_012793.1.
    YP_002949049.1. NC_012793.1.

    3D structure databases

    ProteinModelPortali C5D802.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 471223.GWCH70_0919.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACS23783 ; ACS23783 ; GWCH70_0919 .
    GeneIDi 7976647.
    KEGGi gwc:GWCH70_0919.
    PATRICi 21970752. VBIGeoSp101709_0991.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci GSP471223:GH2C-1003-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: WCH70.

    Entry informationi

    Entry nameiODO1_GEOSW
    AccessioniPrimary (citable) accession number: C5D802
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 38 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