Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O58045

- IMDH_PYRHO

UniProt

O58045 - IMDH_PYRHO

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 2991IMP
    Active sitei301 – 3011Thioimidate intermediateUniRule annotation
    Metal bindingi301 – 3011Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei412 – 4121IMP
    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

    BioCyciPHOR70601:GJWR-289-MONOMER.
    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:PH0307
    OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
    Taxonomic identifieri70601 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000000752: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Inosine-5'-monophosphate dehydrogenasePRO_0000093722Add
    BLAST

    Proteomic databases

    PRIDEiO58045.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi70601.PH0307.

    Structurei

    Secondary structure

    1
    486
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 96
    Helixi17 – 193
    Beta strandi20 – 223
    Beta strandi38 – 414
    Beta strandi44 – 529
    Turni56 – 583
    Helixi61 – 699
    Beta strandi73 – 764
    Beta strandi78 – 803
    Helixi82 – 9312
    Beta strandi222 – 2254
    Helixi230 – 2389
    Beta strandi242 – 2476
    Helixi254 – 26512
    Beta strandi269 – 2768
    Helixi279 – 2824
    Beta strandi288 – 2936
    Helixi303 – 3064
    Helixi313 – 32614
    Beta strandi330 – 3356
    Helixi340 – 3489
    Beta strandi352 – 3576
    Turni358 – 3625
    Beta strandi370 – 3734
    Beta strandi376 – 3827
    Helixi387 – 3904
    Beta strandi415 – 4195
    Helixi424 – 44118
    Helixi447 – 4537
    Beta strandi456 – 4583
    Helixi461 – 4677

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CU0X-ray2.10A/B1-486[»]
    ProteinModelPortaliO58045.
    SMRiO58045. Positions 3-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO58045.

    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 binding
    Regioni357 – 3582IMP binding
    Regioni381 – 3855IMP binding

    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.
    OMAiYEALTFD.

    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.

    O58045-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKFVEKLEK AIKGYTFDDV LLIPQATEVE PKDVDVSTRI TPNVKLNIPI    50
    LSAAMDTVTE WEMAVAMARE GGLGVIHRNM GIEEQVEQVK RVKRAERLIV 100
    EDVITIAPDE TVDFALFLME KHGIDGLPVV EDEKVVGIIT KKDIAAREGK 150
    LVKELMTKEV ITVPESIEVE EALKIMIENR IDRLPVVDER GKLVGLITMS 200
    DLVARKKYKN AVRDENGELL VAAAVSPFDI KRAIELDKAG VDVIVVDTAH 250
    AHNLKAIKSM KEMRQKVDAD FIVGNIANPK AVDDLTFADA VKVGIGPGSI 300
    CTTRIVAGVG VPQITAVAMV ADRAQEYGLY VIADGGIRYS GDIVKAIAAG 350
    ADAVMLGNLL AGTKEAPGKE VIINGRKYKQ YRGMGSLGAM MKGGAERYYQ 400
    GGYMKTRKFV PEGVEGVVPY RGTVSEVLYQ LVGGLKAGMG YVGARNIREL 450
    KEKGEFVIIT HAGIKESHPH DIIITNEAPN YPLEKF 486
    Length:486
    Mass (Da):52,933
    Last modified:August 1, 1998 - v1
    Checksum:i6B21E9B7B3AA7C3C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000001 Genomic DNA. Translation: BAA29380.1.
    PIRiE71456.
    RefSeqiNP_142293.1. NC_000961.1.

    Genome annotation databases

    EnsemblBacteriaiBAA29380; BAA29380; BAA29380.
    GeneIDi1444188.
    KEGGipho:PH0307.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000001 Genomic DNA. Translation: BAA29380.1 .
    PIRi E71456.
    RefSeqi NP_142293.1. NC_000961.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CU0 X-ray 2.10 A/B 1-486 [» ]
    ProteinModelPortali O58045.
    SMRi O58045. Positions 3-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 70601.PH0307.

    Proteomic databases

    PRIDEi O58045.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA29380 ; BAA29380 ; BAA29380 .
    GeneIDi 1444188.
    KEGGi pho:PH0307.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci PHOR70601:GJWR-289-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O58045.

    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: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
    2. "Crystal structure of inosine-5'-monophosphate dehydrogenase from Pyrococcus horikoshii OT3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH XMP.
      Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

    Entry informationi

    Entry nameiIMDH_PYRHO
    AccessioniPrimary (citable) accession number: O58045
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 107 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

    3D-structure, Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3