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Q9KTW3

- Q9KTW3_VIBCH

UniProt

Q9KTW3 - Q9KTW3_VIBCH

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Oct 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 sitei256 – 2561NADImported
    Binding sitei279 – 2791NADImported
    Metal bindingi302 – 3021Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi304 – 3041Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei305 – 3051IMPUniRule annotation
    Active sitei307 – 3071Thioimidate intermediateUniRule annotation
    Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei417 – 4171IMPUniRule annotation
    Binding sitei442 – 4421NADImported
    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 bindingi250 – 2523NADUniRule annotation
    Nucleotide bindingi250 – 2523NADImported
    Nucleotide bindingi300 – 3023NADUniRule annotation
    Nucleotide bindingi300 – 3023NADImported

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. IMP dehydrogenase activity Source: TIGR
    3. metal ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP
    2. purine ribonucleotide biosynthetic process Source: TIGR

    Keywords - Molecular functioni

    OxidoreductaseUniRule annotation

    Keywords - Biological processi

    GMP biosynthesisUniRule annotation, Purine biosynthesis

    Keywords - Ligandi

    Metal-bindingUniRule annotation, NADUniRule annotationImported, Nucleotide-bindingImported, PotassiumUniRule annotation

    Enzyme and pathway databases

    BioCyciVCHO:VC0767-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:VC_0767Imported
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)Imported
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000584: Chromosome 1

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243277.VC0767.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FEZX-ray2.16A/B1-92[»]
    A/B200-489[»]
    4FO4X-ray2.03A/B1-90[»]
    A/B220-489[»]
    4FXSX-ray2.24A1-489[»]
    4HLVX-ray2.32A/B1-90[»]
    A/B220-489[»]
    4IX2X-ray2.15A/B/C/D1-90[»]
    A/B/C/D220-489[»]
    ProteinModelPortaliQ9KTW3.
    SMRiQ9KTW3. Positions 5-487.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini95 – 15460CBS 1UniRule annotationAdd
    BLAST
    Domaini155 – 21662CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni340 – 3423IMP bindingUniRule annotation
    Regioni363 – 3642IMP bindingUniRule annotation
    Regioni387 – 3915IMP 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

    KOiK00088.
    OMAiHGHSKNI.
    OrthoDBiEOG6GTZPV.

    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.

    Q9KTW3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHMLRIAKEA LTFDDVLLVP AHSTVLPNTA DLRTRLTKNI ALNIPMVSAS    50
    MDTVTEARLA IALAQEGGIG FIHKNMSIEQ QAAQVHQVKI FEAGVVTHPV 100
    TVRPEQTIAD VMELTHYHGF AGFPVVTENN ELVGIITGRD VRFVTDLTKS 150
    VAAVMTPKER LATVKEGATG AEVQEKMHKA RVEKILVVND EFQLKGMITA 200
    KDFHKAESKP NACKDEQGRL RVGAAVGAAP GNEERVKALV EAGVDVLLID 250
    SSHGHSEGVL QRIRETRAAY PHLEIIGGNV ATAEGARALI EAGVSAVKVG 300
    IGPGSICTTR IVTGVGVPQI TAIADAAGVA NEYGIPVIAD GGIRFSGDIS 350
    KAIAAGASCV MVGSMFAGTE EAPGEVILYQ GRSYKAYRGM GSLGAMSKGS 400
    SDRYFQTDNA ADKLVPEGIE GRIAYKGHLK EIIHQQMGGL RSCMGLTGSA 450
    TVEDLRTKAQ FVRISGAGMK ESHVHDVQIT KEAPNYRLG 489
    Length:489
    Mass (Da):51,943
    Last modified:October 1, 2000 - v1
    Checksum:iB38133B52F8661C4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF93932.1.
    PIRiC82282.
    RefSeqiNP_230416.1. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF93932; AAF93932; VC_0767.
    GeneIDi2615310.
    KEGGivch:VC0767.
    PATRICi20080645. VBIVibCho83274_0731.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF93932.1 .
    PIRi C82282.
    RefSeqi NP_230416.1. NC_002505.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FEZ X-ray 2.16 A/B 1-92 [» ]
    A/B 200-489 [» ]
    4FO4 X-ray 2.03 A/B 1-90 [» ]
    A/B 220-489 [» ]
    4FXS X-ray 2.24 A 1-489 [» ]
    4HLV X-ray 2.32 A/B 1-90 [» ]
    A/B 220-489 [» ]
    4IX2 X-ray 2.15 A/B/C/D 1-90 [» ]
    A/B/C/D 220-489 [» ]
    ProteinModelPortali Q9KTW3.
    SMRi Q9KTW3. Positions 5-487.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243277.VC0767.

    Protocols and materials databases

    DNASUi 2615310.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF93932 ; AAF93932 ; VC_0767 .
    GeneIDi 2615310.
    KEGGi vch:VC0767.
    PATRICi 20080645. VBIVibCho83274_0731.

    Phylogenomic databases

    KOi K00088.
    OMAi HGHSKNI.
    OrthoDBi EOG6GTZPV.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci VCHO:VC0767-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39315 / El Tor Inaba N16961Imported.
    2. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant."
      Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
      Submitted (MAY-2012) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 1-92 AND 200-489.
    3. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP and mycophenolic acid."
      Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
      Submitted (JUN-2012) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-90 AND 220-489.
    4. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae complexed with IMP and mycophenolic acid."
      Osipiuk J., Maltseva N., Makowska-Grzyska M., Jedrzejczak R., Anderson W.F., Joachimiak A.
      Submitted (JUL-2012) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS).
    5. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, in complex with NAD and IMP."
      Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
      Submitted (OCT-2012) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 1-90 AND 220-489 IN COMPLEX WITH NAD.
    6. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP."
      Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
      Submitted (JAN-2013) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-90 AND 220-489.

    Entry informationi

    Entry nameiQ9KTW3_VIBCH
    AccessioniPrimary (citable) accession number: Q9KTW3
    Entry historyi
    Integrated into UniProtKB/TrEMBL: October 1, 2000
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 93 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