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Q5WG56

- ODO1_BACSK

UniProt

Q5WG56 - ODO1_BACSK

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Bacillus clausii (strain KSM-K16)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (23 Nov 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

    BioCyciBCLA66692:GHMP-2182-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:ABC2114
    OrganismiBacillus clausii (strain KSM-K16)
    Taxonomic identifieri66692 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001168: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9439432-oxoglutarate dehydrogenase E1 componentPRO_0000162168Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi66692.ABC2114.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5WG56.
    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.

    Q5WG56-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSKEHSPEK PWRGFYGPNL GAVIELYDQY VEDPNSVDEQ TRAHFEKWGP    50
    PALEENVSSS NAKETIGADM ISAVVGAVRL ADYIRAKGHL VSDIQPIWKT 100
    DKNSNLLDYD RFNVTEEELK KVPVKLICKD APPHLKNGLE AIEHLKKVYT 150
    QTMAFEFGHV QDEEERNWLR KQVESEAYAD ELPNKEKKAL LERLTSVEGF 200
    EKFIHRTFVG QKRFSIEGLD TLVPMLDKAI REVRKEKTDH VMIGMAHRGR 250
    LNVLAHTLGK PYKAIFSEFL QAPNKLNAPS EGLGETYTGW TGDVKYHLGA 300
    DRQISDDKSA QTIVSLANNP SHLEFVSPIV EGYARAAQED RSSKGAPKQD 350
    TTRAYSILIH GDAAFPGQGV VTETLNLSRL NGYHVGGSLH IIANNNIGYT 400
    TEMHDSRSTT YASDPAKGFE IPIVHVNADD AEACVRAIKF AVEYRRKFQK 450
    DFLIDLIGYR RFGHNEGDEP AVTQPDLYAQ IRKHPTVRAI YAKQLEAEQV 500
    ITAKEAQKLD TDMYNYLLEE YNKVNSDKSE KKYELSPPDF IVDGLPKVKT 550
    AVEKEKLVAM NEQLLDWPSS FKPNQKLEKI LKRRANAFDG EGNVDWGLAE 600
    ILAFASILHD GTPVRLSGQD SERGTFAHRH FVLHDRETNE THVPLQTIKD 650
    ANASFAVYNS PLTEQACVGF EYGYNVFSKE TLVLWEAQFG DFVNGAQVMF 700
    DQWVSAGRAK WGQKSGLVVL LPHGYEGAGP EHSSGRVERF LSSAAENNWT 750
    VANCTSAAQY FHILRRQAKI LQKNTVRPLI IMTPKSLLRN QVVASPTSAF 800
    TEGEFQPILE EPTLGHDPNA VKRIILCSGK LAIELQDYVN KNDEDWSWVH 850
    IIRVEELYPF PRRAIRERLK EFPNLEEVKW VQEEPKNMGA WTFMEPRIRE 900
    ILPSGVPLSY IGRTYRSSPA EGVSNAHKVE QKRIVTESLT RKN 943
    Length:943
    Mass (Da):106,584
    Last modified:November 23, 2004 - v1
    Checksum:i3FF67A61E3A2C6D8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006627 Genomic DNA. Translation: BAD64649.1.
    RefSeqiYP_175610.1. NC_006582.1.

    Genome annotation databases

    EnsemblBacteriaiBAD64649; BAD64649; ABC2114.
    GeneIDi3202055.
    KEGGibcl:ABC2114.
    PATRICi18923786. VBIBacCla58185_2256.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006627 Genomic DNA. Translation: BAD64649.1 .
    RefSeqi YP_175610.1. NC_006582.1.

    3D structure databases

    ProteinModelPortali Q5WG56.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 66692.ABC2114.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD64649 ; BAD64649 ; ABC2114 .
    GeneIDi 3202055.
    KEGGi bcl:ABC2114.
    PATRICi 18923786. VBIBacCla58185_2256.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BCLA66692:GHMP-2182-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 the alkaliphilic Bacillus clausii KSM-K16."
      Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: KSM-K16.

    Entry informationi

    Entry nameiODO1_BACSK
    AccessioniPrimary (citable) accession number: Q5WG56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 64 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