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Q9KH33

- IMDH_RHITR

UniProt

Q9KH33 - IMDH_RHITR

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Rhizobium tropici
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    • 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 sitei253 – 2531NADUniRule annotation
    Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei308 – 3081IMPUniRule annotation
    Active sitei310 – 3101Thioimidate intermediateUniRule annotation
    Metal bindingi310 – 3101Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei421 – 4211IMPUniRule annotation
    Metal bindingi475 – 4751Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi476 – 4761Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi477 – 4771Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi303 – 3053NADUniRule 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
    OrganismiRhizobium tropici
    Taxonomic identifieri398 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 498498Inosine-5'-monophosphate dehydrogenasePRO_0000093704Add
    BLAST

    Proteomic databases

    PRIDEiQ9KH33.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ9KH33.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini98 – 15558CBS 1UniRule annotationAdd
    BLAST
    Domaini159 – 21658CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni343 – 3453IMP bindingUniRule annotation
    Regioni366 – 3672IMP bindingUniRule annotation
    Regioni390 – 3945IMP bindingUniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domain, Repeat

    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.

    Q9KH33-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARIIETSTG LDALTFDDVL LQPGHSEVMP GQTNIATRIA QDIELNVPIL    50
    SAAMDTVTES RLAIAMAQAG GMGVIHRNLT PVQQAEEVRQ VKKFESGMVV 100
    NPVTIGPDAT LAEALSLDEG PRHFRASPVV EKSHRLVGIL TNRDVRFASD 150
    PEQKIYELMT RENLVTVKDG VQQHEAKRLL HTHRIEKXLV VDADSRFVGL 200
    ITVKDIEKSQ LNPHASKDAQ GRLRAAAAIS VGDDGYERAE RLIDAGVDLL 250
    VVDTAHGHSQ RVLDAVTRVK KLSNSVRIMA GNVATYDGTR ALIDAGADAV 300
    KVGIGPGSIC TTRIVAGVGV PQLAAIMSAV QAAQDQNIPI IADGGIKFSG 350
    DLAKAIAAGA SAAMIGSLLA GTDESPGEVY LYQGRSFKAY RGMGSVGAMA 400
    RGSADRYFQA EVRDTLKLVP EGIEGXVPYK GPVSGVLHQL AGGLKAAMGY 450
    VGGADLKDFQ ERATFVRISG AGLRESHAHD VTITPRKARI IPAQAADR 498
    Length:498
    Mass (Da):52,838
    Last modified:October 1, 2000 - v1
    Checksum:i0A99E38B1078ED73
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF272827 Genomic DNA. Translation: AAF85967.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF272827 Genomic DNA. Translation: AAF85967.1 .

    3D structure databases

    ProteinModelPortali Q9KH33.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9KH33.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "A guaB mutant strain of Rhizobium tropici CIAT899 pleiotropically defective in thermal tolerance and symbiosis."
      Riccillo P.M., Collavino M.M., Grasso D.H., England R., de Bruijn F.J., Aguilar O.M.
      Mol. Plant Microbe Interact. 13:1228-1236(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 899.

    Entry informationi

    Entry nameiIMDH_RHITR
    AccessioniPrimary (citable) accession number: Q9KH33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3