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P42851

- IMDH_PYRFU

UniProt

P42851 - IMDH_PYRFU

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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
    Binding sitei247 – 2471NADUniRule annotation
    Metal bindingi296 – 2961Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi298 – 2981Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei299 – 2991IMPUniRule annotation
    Active sitei301 – 3011Thioimidate intermediateUniRule annotation
    Metal bindingi301 – 3011Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei412 – 4121IMPUniRule annotation
    Metal bindingi466 – 4661Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi467 – 4671Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi468 – 4681Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi294 – 2963NADUniRule 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
    Name:guaBUniRule annotation
    Ordered Locus Names:PF0285
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000001013: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Inosine-5'-monophosphate dehydrogenasePRO_0000093721Add
    BLAST

    Proteomic databases

    PRIDEiP42851.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi186497.PF0285.

    Structurei

    3D structure databases

    ProteinModelPortaliP42851.
    SMRiP42851. Positions 3-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini99 – 15456CBS 1UniRule annotationAdd
    BLAST
    Domaini156 – 21257CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni334 – 3363IMP bindingUniRule annotation
    Regioni357 – 3582IMP bindingUniRule annotation
    Regioni381 – 3855IMP 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.
    HOGENOMiHOG000165755.
    KOiK00088.
    OMAiNAIRGYT.

    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.

    P42851-1 [UniParc]FASTAAdd to Basket

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    MGKFVEKLEN AIRGYTFDDV LLIPQPTEVE PKDVDVSTQI TPNVKLNIPI    50
    LSAAMDTVTE WEMAVAMARE GGLGVIHRNM SIEEQVEQVK RVKRAERFIV 100
    EDVITIAPDE TIDYALFLME KHGIDGLPVV EEDRVVGIIT KKDIAAREGR 150
    TVKELMTREV ITVPESVDVE EALKIMMENR IDRLPVVNED GKLVGLITMS 200
    DLVARKKYKN AVRNEKGELL VAAAVSPFDL RRAIELDRAG VDVIVVDTAH 250
    AHNLKAIKAM KEMRQKVSAD FIVGNIANPK AVDDLTFADA VKVGIGPGSI 300
    CTTRIVAGVG VPQITAIAMV ADRAQEYGLY VIADGGIKYS GDIVKAIAAG 350
    ADAVMLGNLL AGTKEAPGKE VIINGRKYKQ YRGMGSLGAM MKGGAERYYQ 400
    GGYMKTRKFV PEGVEGVVPY RGTVSEVLYQ LVGGLKAGMG YVGARNIKEL 450
    KEKGEFVIIT SAGLRESHPH DIIITNEAPN YPLER 485
    Length:485
    Mass (Da):52,900
    Last modified:November 1, 1995 - v1
    Checksum:iBDA60E0D349E5B5B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08814 Genomic DNA. Translation: AAC44532.1.
    AE009950 Genomic DNA. Translation: AAL80409.1.
    PIRiJC4998.
    RefSeqiNP_578014.1. NC_003413.1.
    WP_011011399.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL80409; AAL80409; PF0285.
    GeneIDi1468119.
    KEGGipfu:PF0285.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08814 Genomic DNA. Translation: AAC44532.1 .
    AE009950 Genomic DNA. Translation: AAL80409.1 .
    PIRi JC4998.
    RefSeqi NP_578014.1. NC_003413.1.
    WP_011011399.1. NC_003413.1.

    3D structure databases

    ProteinModelPortali P42851.
    SMRi P42851. Positions 3-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 186497.PF0285.

    Proteomic databases

    PRIDEi P42851.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL80409 ; AAL80409 ; PF0285 .
    GeneIDi 1468119.
    KEGGi pfu:PF0285.

    Phylogenomic databases

    eggNOGi COG0517.
    HOGENOMi HOG000165755.
    KOi K00088.
    OMAi NAIRGYT.

    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. "Cloning, characterization and sequence comparison of the gene coding for IMP dehydrogenase from Pyrococcus furiosus."
      Collart F.R., Osipiuk J., Trent J., Olsen G.J., Huberman E.
      Gene 174:209-216(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

    Entry informationi

    Entry nameiIMDH_PYRFU
    AccessioniPrimary (citable) accession number: P42851
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 110 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3