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Q9HXM5

- Q9HXM5_PSEAE

UniProt

Q9HXM5 - Q9HXM5_PSEAE

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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 sitei98 – 981ATP; via amide nitrogen and carbonyl oxygenImported
    Binding sitei153 – 1531ATPImported
    Binding sitei159 – 1591ATP; via amide nitrogen and carbonyl oxygenImported
    Binding sitei247 – 2471NADUniRule annotation
    Metal bindingi299 – 2991Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi301 – 3011Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei302 – 3021IMPUniRule annotation
    Active sitei304 – 3041Thioimidate intermediateUniRule annotation
    Metal bindingi304 – 3041Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei417 – 4171IMPUniRule annotation
    Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi472 – 4721Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi473 – 4731Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi118 – 1203ATPImported
    Nucleotide bindingi134 – 1374ATPImported
    Nucleotide bindingi180 – 1812ATPImported
    Nucleotide bindingi198 – 1992ATPImported
    Nucleotide bindingi297 – 2993NADUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    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

    OxidoreductaseUniRule annotation

    Keywords - Biological processi

    GMP biosynthesisUniRule annotation, Purine biosynthesis

    Keywords - Ligandi

    ATP-bindingImported, Metal-bindingUniRule annotation, NADUniRule annotation, Nucleotide-binding, PotassiumUniRule annotation

    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 annotationImported
    Ordered Locus Names:PA3770Imported
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)Imported
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA3770.

    PTM / Processingi

    Proteomic databases

    PRIDEiQ9HXM5.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    DIPiDIP-60162N.
    STRINGi208964.PA3770.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZFHX-ray2.25A1-489[»]
    4AVFX-ray2.23A/B/C/D1-489[»]
    4DQWX-ray2.51A/B1-489[»]
    ProteinModelPortaliQ9HXM5.
    SMRiQ9HXM5. Positions 1-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini93 – 14856CBS 1UniRule annotationAdd
    BLAST
    Domaini152 – 21059CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni337 – 3393IMP bindingUniRule annotation
    Regioni360 – 3612IMP bindingUniRule annotation
    Regioni384 – 3885IMP bindingUniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domainUniRule annotation, RepeatUniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000165755.
    KOiK00088.
    OMAiNNSQKRY.
    OrthoDBiEOG6GTZPV.
    PhylomeDBiQ9HXM5.

    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.

    Q9HXM5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRISQEALT FDDVLLIPGY SEVLPKDVSL KTRLTRGIEL NIPLVSAAMD    50
    TVTEARLAIA MAQEGGIGII HKNMGIEQQA AEVRKVKKHE TAIVRDPVTV 100
    TPSTKIIELL QMAREYGFSG FPVVEQGELV GIVTGRDLRV KPNAGDTVAA 150
    IMTPKDKLVT AREGTPLEEM KAKLYENRIE KMLVVDENFY LRGLVTFRDI 200
    EKAKTYPLAS KDEQGRLRVG AAVGTGADTG ERVAALVAAG VDVVVVDTAH 250
    GHSKGVIERV RWVKQTFPDV QVIGGNIATA EAAKALAEAG ADAVKVGIGP 300
    GSICTTRIVA GVGVPQISAI ANVAAALEGT GVPLIADGGI RFSGDLAKAM 350
    VAGAYCVMMG SMFAGTEEAP GEIELFQGRS YKSYRGMGSL GAMSGSQGSS 400
    DRYFQDASAG AEKLVPEGIE GRVPYKGALS AIVHQLMGGL RAAMGYTGSA 450
    DIQQMRTQPQ FVRITGAGMA ESHVHDVQIT KEAPNYRVG 489
    Length:489
    Mass (Da):51,707
    Last modified:March 1, 2001 - v1
    Checksum:i6D2320AFD52C888B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG07157.1.
    PIRiH83173.
    RefSeqiNP_252459.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG07157; AAG07157; PA3770.
    GeneIDi880535.
    KEGGipae:PA3770.
    PATRICi19842179. VBIPseAer58763_3947.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG07157.1 .
    PIRi H83173.
    RefSeqi NP_252459.1. NC_002516.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZFH X-ray 2.25 A 1-489 [» ]
    4AVF X-ray 2.23 A/B/C/D 1-489 [» ]
    4DQW X-ray 2.51 A/B 1-489 [» ]
    ProteinModelPortali Q9HXM5.
    SMRi Q9HXM5. Positions 1-468.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60162N.
    STRINGi 208964.PA3770.

    Proteomic databases

    PRIDEi Q9HXM5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG07157 ; AAG07157 ; PA3770 .
    GeneIDi 880535.
    KEGGi pae:PA3770.
    PATRICi 19842179. VBIPseAer58763_3947.

    Organism-specific databases

    PseudoCAPi PA3770.

    Phylogenomic databases

    HOGENOMi HOG000165755.
    KOi K00088.
    OMAi NNSQKRY.
    OrthoDBi EOG6GTZPV.
    PhylomeDBi Q9HXM5.

    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: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228Imported.
    2. "The AEROPATH project targeting Pseudomonas aeruginosa: crystallographic studies for assessment of potential targets in early-stage drug discovery."
      Moynie L., Schnell R., McMahon S.A., Sandalova T., Boulkerou W.A., Schmidberger J.W., Alphey M., Cukier C., Duthie F., Kopec J., Liu H., Jacewicz A., Hunter W.N., Naismith J.H., Schneider G.
      Acta Crystallogr. F 69:25-34(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS).
    3. "Structure of Pseudomonas aeruginosa inosine 5'-monophosphate dehydrogenase."
      Rao V.A., Shepherd S.M., Owen R., Hunter W.N.
      Acta Crystallogr. F 69:243-247(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    4. "MgATP regulates allostery and fiber formation in IMPDHs."
      Labesse G., Alexandre T., Vaupre L., Salard-Arnaud I., Him J.L., Raynal B., Bron P., Munier-Lehmann H.
      Structure 21:975-985(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) IN COMPLEX WITH ATP.

    Entry informationi

    Entry nameiQ9HXM5_PSEAE
    AccessioniPrimary (citable) accession number: Q9HXM5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 1, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3