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E6ULW2

- E6ULW2_CLOTL

UniProt

E6ULW2 - E6ULW2_CLOTL

Protein

Isocitrate dehydrogenase [NADP]

Gene

Clo1313_1944

Organism
Clostridium thermocellum (strain DSM 1313 / LMG 6656 / LQ8) (Ruminiclostridium thermocellum)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (08 Mar 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.UniRule annotation

    Cofactori

    Binds 1 magnesium or manganese ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei77 – 771Substrate
    Binding sitei109 – 1091Substrate
    Binding sitei132 – 1321SubstrateUniRule annotation
    Sitei139 – 1391Critical for catalysisUniRule annotation
    Sitei210 – 2101Critical for catalysisUniRule annotation
    Metal bindingi250 – 2501Magnesium or manganeseUniRule annotation
    Metal bindingi273 – 2731Magnesium or manganeseUniRule annotation

    GO - Molecular functioni

    1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB-EC
    2. magnesium ion binding Source: InterPro
    3. NAD binding Source: InterPro

    GO - Biological processi

    1. isocitrate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    OxidoreductaseUniRule annotation

    Keywords - Biological processi

    Tricarboxylic acid cycleUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, ManganeseUniRule annotation, Metal-bindingUniRule annotation, NADPUniRule annotation

    Enzyme and pathway databases

    BioCyciCTHE637887:GLBN-1992-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NADP]UniRule annotation (EC:1.1.1.42UniRule annotation)
    Gene namesi
    Ordered Locus Names:Clo1313_1944Imported
    OrganismiClostridium thermocellum (strain DSM 1313 / LMG 6656 / LQ8) (Ruminiclostridium thermocellum)Imported
    Taxonomic identifieri637887 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
    ProteomesiUP000008083: Chromosome

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AOYX-ray2.35A/B/C/D1-402[»]
    ProteinModelPortaliE6ULW2.
    SMRiE6ULW2. Positions 3-401.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni94 – 1007Substrate binding

    Sequence similaritiesi

    Belongs to the isocitrate and isopropylmalate dehydrogenases family.UniRule annotation

    Phylogenomic databases

    KOiK00031.
    OMAiKNTIMKV.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR004790. Isocitrate_DH_NADP.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view]
    PANTHERiPTHR11822. PTHR11822. 1 hit.
    PfamiPF00180. Iso_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000108. IDH_NADP. 1 hit.
    TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    E6ULW2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKIKMKVPL VEMDGDEMTR IIWRLIKENL LEPYIELNTE YYDLGLENRD    50
    KTEDQVTIDA ARAIQKYGVG VKCATITPNA QRVEEYNLKK MWKSPNGTIR 100
    AILDGTVFRA PIVVNSIKPF VKGWKKPISI ARHAYGDVYK NVEYYVPSAG 150
    KAELVFTSEN GEVSRQTIHE FDGPGVIMGM HNTDKSIRSF ARACFNYALD 200
    MNQDLWFSTK DTISKTYDHR FKDIFQEIYE NEYKEKFEAK NLQYFYTLID 250
    DAVARIIRSE GGMVWACKNY DGDVMSDMVA SAFGSLAMMT SVLVSPDGKY 300
    EFEAAHGTVT RHYYKHLKGE ETSTNSMATI FAWTGALKKR GELDGIKELV 350
    DFATKLEQAS VQTIENGVMT KDLASLSEVP EKKIVNTEDF LKEIRKTFEG 400
    MA 402
    Length:402
    Mass (Da):45,782
    Last modified:March 8, 2011 - v1
    Checksum:i5A55781A7AC5B42E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002416 Genomic DNA. Translation: ADU74991.1.
    RefSeqiYP_005688442.1. NC_017304.1.

    Genome annotation databases

    EnsemblBacteriaiADU74991; ADU74991; Clo1313_1944.
    GeneIDi12421679.
    KEGGictx:Clo1313_1944.
    PATRICi45478813. VBICloThe140364_2116.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002416 Genomic DNA. Translation: ADU74991.1 .
    RefSeqi YP_005688442.1. NC_017304.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AOY X-ray 2.35 A/B/C/D 1-402 [» ]
    ProteinModelPortali E6ULW2.
    SMRi E6ULW2. Positions 3-401.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADU74991 ; ADU74991 ; Clo1313_1944 .
    GeneIDi 12421679.
    KEGGi ctx:Clo1313_1944.
    PATRICi 45478813. VBICloThe140364_2116.

    Phylogenomic databases

    KOi K00031.
    OMAi KNTIMKV.

    Enzyme and pathway databases

    BioCyci CTHE637887:GLBN-1992-MONOMER.

    Family and domain databases

    Gene3Di 3.40.718.10. 1 hit.
    InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR004790. Isocitrate_DH_NADP.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view ]
    PANTHERi PTHR11822. PTHR11822. 1 hit.
    Pfami PF00180. Iso_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000108. IDH_NADP. 1 hit.
    TIGRFAMsi TIGR00127. nadp_idh_euk. 1 hit.
    PROSITEi PS00470. IDH_IMDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 1313 / LMG 6656 / LQ8Imported.
    2. "The complex structures of isocitrate dehydrogenase from Clostridium thermocellum and Desulfotalea psychrophila suggest a new active site locking mechanism."
      Leiros H.K., Fedoy A.E., Leiros I., Steen I.H.
      FEBS Open Bio 2:159-172(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).

    Entry informationi

    Entry nameiE6ULW2_CLOTL
    AccessioniPrimary (citable) accession number: E6ULW2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 8, 2011
    Last sequence update: March 8, 2011
    Last modified: October 1, 2014
    This is version 27 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteomeImported

    External Data

    Dasty 3