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Q9UY49

- IMDH_PYRAB

UniProt

Q9UY49 - IMDH_PYRAB

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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:PYRAB16590
    ORF Names:PAB1250
    OrganismiPyrococcus abyssi (strain GE5 / Orsay)
    Taxonomic identifieri272844 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000000810: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Inosine-5'-monophosphate dehydrogenasePRO_0000093720Add
    BLAST

    Proteomic databases

    PRIDEiQ9UY49.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272844.PAB1250.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UY49.
    SMRiQ9UY49. Positions 3-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini99 – 15456CBS 1UniRule annotationAdd
    BLAST
    Domaini156 – 21560CBS 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.
    OMAiHGHSKNI.

    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.

    Q9UY49-1 [UniParc]FASTAAdd to Basket

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    MGKFAKKLER AIRGYTFDDV LLIPQATEVE PKDVDVSTQI TPNVKLNIPI    50
    LSAAMDTVTE WEMAVAMARE GGLGVIHRNM SIEEQVEQVK RVKKAERFIV 100
    EDVITISPEE TVDFALFLME KHDIDGLPVV ENEKVVGIIS KKDIAAREGK 150
    LVKELMTKDV ITVPENIEVE EALKIMIENR IDRLPVVDKE GRLIGLITMS 200
    DLVARKKYKN AVRDENGELL VAAAVSPFDI RRAIELDRAG ADVIVVDTAH 250
    AHNLKAIKAM KEMRQKVDAD 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 YPLEK 485
    Length:485
    Mass (Da):52,868
    Last modified:May 1, 2000 - v1
    Checksum:iFF3DDB8521FC7113
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ248288 Genomic DNA. Translation: CAB50563.1.
    HE613800 Genomic DNA. Translation: CCE71127.1.
    PIRiE75015.
    RefSeqiNP_127333.1. NC_000868.1.
    WP_010868777.1. NC_000868.1.

    Genome annotation databases

    EnsemblBacteriaiCAB50563; CAB50563; PAB1250.
    GeneIDi1495956.
    KEGGipab:PAB1250.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ248288 Genomic DNA. Translation: CAB50563.1 .
    HE613800 Genomic DNA. Translation: CCE71127.1 .
    PIRi E75015.
    RefSeqi NP_127333.1. NC_000868.1.
    WP_010868777.1. NC_000868.1.

    3D structure databases

    ProteinModelPortali Q9UY49.
    SMRi Q9UY49. Positions 3-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272844.PAB1250.

    Proteomic databases

    PRIDEi Q9UY49.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB50563 ; CAB50563 ; PAB1250 .
    GeneIDi 1495956.
    KEGGi pab:PAB1250.

    Phylogenomic databases

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

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: GE5 / Orsay.
    2. "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
      Gao J., Wang J.
      Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: GE5 / Orsay.

    Entry informationi

    Entry nameiIMDH_PYRAB
    AccessioniPrimary (citable) accession number: Q9UY49
    Secondary accession number(s): G8ZK20
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 106 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

    Documents

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

    External Data

    Dasty 3