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Q59106

- ODO1_CUPNH

UniProt

Q59106 - ODO1_CUPNH

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (23 Jan 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).

    Catalytic activityi

    2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

    Cofactori

    Thiamine pyrophosphate.

    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

    BioCyciCNEC381666:GJUJ-2293-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenase
    Gene namesi
    Name:odhA
    Ordered Locus Names:H16_A2325
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000008210: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9509502-oxoglutarate dehydrogenase E1 componentPRO_0000162160Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi381666.H16_A2325.

    Structurei

    3D structure databases

    ProteinModelPortaliQ59106.
    SMRiQ59106. Positions 88-941.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0567.
    HOGENOMiHOG000259586.
    KOiK00164.
    OMAiGFTTAPH.
    OrthoDBiEOG6V1M1F.

    Family and domain databases

    Gene3Di3.40.50.970. 2 hits.
    InterProiIPR011603. 2oxoglutarate_DH_E1.
    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.

    Q59106-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMQQYQSNSY LFGGNAPYVE ELYEAYLQNP ASVPDNWRAY FDAMQNVPAV    50
    DGSNGRDIPH APIVASFAER AKQGPIRTIV ASADSDMGRK RVAATQLIAA 100
    YRNIGSHWAD LDPLKRQERP PLPDLDPAFY GFSEADLDIV FNASNTYFGK 150
    ESMSLRELLN NLRETYCGTI GFEFMYVSDQ AQKRWWQERL ETTRSKPVFT 200
    LEKKKHILDR LTAAEGLERF LHTKYVGQKR FSLEGGESFI AAMDELIQHA 250
    GSKGVQEIVI GMAHRGRLNV LVNTLGKMPA DLFAEFEGKH VDDLPAGDVK 300
    YHKGFSSDVS TEGGPVHLSL AFNPSHLEIV NPVVEGSAKA RQERRGEVGH 350
    KEVLPVQVHG DAAFAGQGVV METLNLAQTR GYGTGGSMHI VINNQIGFTT 400
    SDPRDARSTL YCTDVVKMIE APVLHVNGDD PEAVVYAMQL AVDFRMEFKK 450
    DVVVDIICFR KLGHNEQDTP AVTQPLMYKK IAQHPGTRKL YADKLAAQNL 500
    VPAEFGDEKV KAYRAAMDAG KHTADPVLSN FKNKFAVDWM PFLNRKWTDA 550
    ADTAVPVTEL KRLAERITTT PETLKLHPLV EKVVKDRANM GRGDQPLDWG 600
    MGEHLAFASL VSSGYPVRIT GQDAGRGTFT HRHAVLHDQA RERWDAGSYV 650
    PLQNVSENQA PFTVIDSVLS EEAVLGFEYG YSAAEPNALV IWEAQFGDFV 700
    NGAQVVIDQF ISSGEVKWGR ASGLTLMLPH GYEGQGPEHS SARIERFLQL 750
    CADHNMQVCQ PTTPAQIFHL LRRQMIRLFR KPLVIMTPKS LLRNKDAVSP 800
    LSDLAKGHFE TVIPDHEELN ASKVKRVIMC SGKVYYDLVN TRKEREANDT 850
    AVIRLEQLYP FPHKAVAAEL KKYPNATEIV WCQDEPQNQG AWFFVQHYIM 900
    ENMTDGQKLG YAGRPASASP AVGYYAKHNE QQKALLEAAF AKLKGFVLTK 950
    Length:950
    Mass (Da):105,996
    Last modified:January 23, 2007 - v2
    Checksum:i531BC77561D2ECCF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti621 – 6211G → A in CAA62980. (PubMed:8867378)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91877 Genomic DNA. Translation: CAA62980.1.
    AM260479 Genomic DNA. Translation: CAJ93421.1.
    PIRiT44422.
    RefSeqiYP_726789.1. NC_008313.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ93421; CAJ93421; H16_A2325.
    GeneIDi4249723.
    KEGGireh:H16_A2325.
    PATRICi35234169. VBIRalEut6770_2731.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91877 Genomic DNA. Translation: CAA62980.1 .
    AM260479 Genomic DNA. Translation: CAJ93421.1 .
    PIRi T44422.
    RefSeqi YP_726789.1. NC_008313.1.

    3D structure databases

    ProteinModelPortali Q59106.
    SMRi Q59106. Positions 88-941.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 381666.H16_A2325.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ93421 ; CAJ93421 ; H16_A2325 .
    GeneIDi 4249723.
    KEGGi reh:H16_A2325.
    PATRICi 35234169. VBIRalEut6770_2731.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CNEC381666:GJUJ-2293-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.970. 2 hits.
    InterProi IPR011603. 2oxoglutarate_DH_E1.
    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. "Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex."
      Hein S., Steinbuechel A.
      FEMS Microbiol. Lett. 136:231-238(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

    Entry informationi

    Entry nameiODO1_CUPNH
    AccessioniPrimary (citable) accession number: Q59106
    Secondary accession number(s): Q0K9A0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 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