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Q4WHZ9

- IMDH_ASPFU

UniProt

Q4WHZ9 - IMDH_ASPFU

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

AFUA_2G03610

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      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 bindingi344 – 3441Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi346 – 3461Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei347 – 3471IMPUniRule annotation
    Active sitei349 – 3491Thioimidate intermediateUniRule annotation
    Metal bindingi349 – 3491Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei472 – 4721IMPUniRule annotation
    Metal bindingi531 – 5311Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi532 – 5321Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi292 – 2943NADUniRule annotation
    Nucleotide bindingi342 – 3443NADUniRule 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:AFUA_2G03610
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 2

    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 – 546546Inosine-5'-monophosphate dehydrogenasePRO_0000415686Add
    BLAST

    Proteomic databases

    PRIDEiQ4WHZ9.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00003552.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WHZ9.
    SMRiQ4WHZ9. Positions 31-132.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini135 – 19763CBS 1UniRule annotationAdd
    BLAST
    Domaini198 – 25457CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni382 – 3843IMP bindingUniRule annotation
    Regioni405 – 4062IMP bindingUniRule annotation
    Regioni430 – 4345IMP 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

    HOGENOMiHOG000165752.
    KOiK00088.
    OMAiKVKSTMC.
    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]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    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.

    Q4WHZ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPIANGDSLG CAMKADIQDY TKALEILEKE YTTRDGLDVD TLLDSDKHGA    50
    LTYNDFLILP GYIGFPASDV TLDTPVTKRV SLKVPLLSSP MDTVTEHNMA 100
    IHMALLGGLG VIHHNCSPED QAEMVRKVKR YENGFILDPV VLSPKATVGE 150
    AKALKAKWGF GGFPVTENGT LRSKLVGMVT SRDIQFHTNL DDPVTAIMST 200
    DLVTAPAGTT LAEANDVLRS SKKGKLPIVD ADGNLVSLLS RSDLMKNLHY 250
    PLASKLPDSK QLICAAAIGT REEDKHRLKL LVEAGLDIVV LDSSQGNSIY 300
    QIEMIKWVKK TFPEIDVIAG NVVTREQAAA LIAAGADGLR IGMGSGSACI 350
    TQEVMAVGRP QAVAVRSVAS FAARFGVPCI ADGGIQNVGH IVKGLAMGAS 400
    TVMMGGLLAG TTESPGEYFV SNEGQLVKAY RGMGSIAAME DKKAGAGSKD 450
    SKASNAGTAR YFSEKDRVLV AQGVAGSVLD RGSVTKFVPY LVAGVQHSLQ 500
    DIGVKSLDEL HDGVNKGIVR FEMRSASAMA EGNVHGLHSY DKKLYS 546
    Length:546
    Mass (Da):57,959
    Last modified:July 5, 2005 - v1
    Checksum:i1156171C58DCD8AE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000008 Genomic DNA. Translation: EAL87456.1.
    RefSeqiXP_749494.1. XM_744401.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00003552; CADAFUAP00003552; CADAFUAG00003552.
    GeneIDi3507220.
    KEGGiafm:AFUA_2G03610.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000008 Genomic DNA. Translation: EAL87456.1 .
    RefSeqi XP_749494.1. XM_744401.1.

    3D structure databases

    ProteinModelPortali Q4WHZ9.
    SMRi Q4WHZ9. Positions 31-132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00003552.

    Proteomic databases

    PRIDEi Q4WHZ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00003552 ; CADAFUAP00003552 ; CADAFUAG00003552 .
    GeneIDi 3507220.
    KEGGi afm:AFUA_2G03610.

    Phylogenomic databases

    HOGENOMi HOG000165752.
    KOi K00088.
    OMAi KVKSTMC.
    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 ]
    PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
    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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiIMDH_ASPFU
    AccessioniPrimary (citable) accession number: Q4WHZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 69 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