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Q7SFX7

- IMDH_NEUCR

UniProt

Q7SFX7 - IMDH_NEUCR

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

NCU03117

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.UniRule annotation

    Catalytic activityi

    Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

    Cofactori

    Potassium.UniRule annotation

    Enzyme regulationi

    Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi335 – 3351Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi337 – 3371Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei338 – 3381IMPUniRule annotation
    Active sitei340 – 3401Thioimidate intermediateUniRule annotation
    Metal bindingi340 – 3401Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei463 – 4631IMPUniRule annotation
    Metal bindingi522 – 5221Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi523 – 5231Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi524 – 5241Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi283 – 2853NADUniRule annotation
    Nucleotide bindingi333 – 3353NADUniRule annotation

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
    3. metal ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenaseUniRule annotation
    Short name:
    IMPDUniRule annotation
    Short name:
    IMPDHUniRule annotation
    Gene namesi
    ORF Names:NCU03117
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 1, Linkage Group I

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 536536Inosine-5'-monophosphate dehydrogenasePRO_0000415687Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi5141.NCU03117.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7SFX7.
    SMRiQ7SFX7. Positions 22-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini126 – 18762CBS 1UniRule annotationAdd
    BLAST
    Domaini189 – 24557CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni373 – 3753IMP bindingUniRule annotation
    Regioni396 – 3972IMP bindingUniRule annotation
    Regioni421 – 4255IMP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 2 CBS domains.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.
    HOGENOMiHOG000165752.
    KOiK00088.
    OMAiHGHSKNI.
    OrthoDBiEOG793BHK.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PfamiPF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    SMARTiSM00116. CBS. 2 hits.
    [Graphical view]
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7SFX7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVNGNNTFL DHTSAMEVLK EYERRDGLDI RDLMDSKLQG GLTYNDFLLL    50
    PGYIGFPASA VTLDSPITKR ITLKTPLVSS PMDTVTEHEM AIHMALQGGV 100
    GVIHHNCSPD EQADMVRKVK RYENGFILDP VVITRDTTVG EAKALKEKWG 150
    FGGFPVTESG NLGSKLVGIV TNRDIQFETD LDKPVSEVMV TDLITATAGV 200
    NLLEANKILA ESKKGKLPII DKEGNLVSMI SRSDLTKNLH FPLASKTKDS 250
    KQLICAAAIG TRPEDKDRLA KLVDAGLDIV ILDSSQGNSM YQIEMIKWIK 300
    KEFPDLDVIG GNVVTREQAA ALIAAGVDGL RIGMGSGSAC ITQEVMAVGR 350
    PQATAVYNVS SFAARFGVPC IADGGIQNVG HIVKGLALGA STVMMGGLLA 400
    GTTESPGTSF VSREGKLVKA YRGMGSIDAM QDKKAGGGGK DAQKSNAGTA 450
    RYFSEGDSIL VAQGVSGAVA HRGSINKFVP YLAAGLKHSL QDCGMTSLQE 500
    LHECVENGTV RFEIRTASAQ LEGGVNMESY EKKLYA 536
    Length:536
    Mass (Da):57,159
    Last modified:December 15, 2003 - v1
    Checksum:iA18ED8F90E4748AB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM002236 Genomic DNA. Translation: EAA35740.1.
    RefSeqiXP_964976.1. XM_959883.2.
    UniGeneiNcr.24401.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000003006; EFNCRP00000003006; EFNCRG00000003003.
    GeneIDi3881134.
    KEGGincr:NCU03117.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM002236 Genomic DNA. Translation: EAA35740.1 .
    RefSeqi XP_964976.1. XM_959883.2.
    UniGenei Ncr.24401.

    3D structure databases

    ProteinModelPortali Q7SFX7.
    SMRi Q7SFX7. Positions 22-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU03117.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000003006 ; EFNCRP00000003006 ; EFNCRG00000003003 .
    GeneIDi 3881134.
    KEGGi ncr:NCU03117.

    Phylogenomic databases

    eggNOGi COG0517.
    HOGENOMi HOG000165752.
    KOi K00088.
    OMAi HGHSKNI.
    OrthoDBi EOG793BHK.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01964. IMPDH.
    InterProi IPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    Pfami PF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000130. IMPDH. 1 hit.
    SMARTi SM00116. CBS. 2 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
    PROSITEi PS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

    Entry informationi

    Entry nameiIMDH_NEUCR
    AccessioniPrimary (citable) accession number: Q7SFX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3