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Q4VRV8

- IMDH_TOXGO

UniProt

Q4VRV8 - IMDH_TOXGO

Protein

Inosine-5'-monophosphate dehydrogenase

Gene
N/A
Organism
Toxoplasma gondii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      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.1 PublicationUniRule 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. Potently inhibited by MPA and adenine dinucleotide analogs such as thiazole-4-carboxamide adenine dinucleotide (TAD).1 PublicationUniRule annotation

    Kineticsi

    1. KM=144 µM for NAD+1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi310 – 3101Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi312 – 3121Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei313 – 3131IMPUniRule annotation
    Active sitei315 – 3151Thioimidate intermediateUniRule annotation
    Metal bindingi315 – 3151Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei477 – 4771IMPUniRule annotation
    Metal bindingi536 – 5361Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi537 – 5371Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi258 – 2603NADUniRule annotation
    Nucleotide bindingi308 – 3103NADUniRule 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

    BRENDAi1.1.1.205. 262552.
    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
    OrganismiToxoplasma gondii
    Taxonomic identifieri5811 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 551551Inosine-5'-monophosphate dehydrogenasePRO_0000415683Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ4VRV8.
    SMRiQ4VRV8. Positions 211-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini102 – 16362CBS 1UniRule annotationAdd
    BLAST
    Domaini165 – 22157CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni349 – 3513IMP bindingUniRule annotation
    Regioni372 – 3732IMP bindingUniRule annotation
    Regioni396 – 4005IMP 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. 2 hits.
    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. 2 hits.
    [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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform TgIMPDH (identifier: Q4VRV8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MADGWDAEKI FNTTVFGFTY DDLILMPGHI DFGVNDVDLS TRITRNLHVR    50
    TPIVSSPMDT VTEHRMAIGC ALMGGMGVIH NNMETARQVA EVQKVKRYEN 100
    GFILDPFVLR PSDSVADVYR IKEKYGYSSV PITDTGMLGG KLLGIVTSRD 150
    IDFLTDVHTP LSEVMTSDLV VGHEPVQLAE ANELLRESKK GKLPIVNDNF 200
    ELVALISRND LKKNREFPLA SKDSNKQLLV GAAVSTKPHD IERAKALQEA 250
    GADVLVVDSS QGDSIYQVDL VKRLKAAFPE LQIIGGNVVT ARQAKSLIDA 300
    GVDGLRIGMG SGSICTTQVV CAVGRAQATA VYHVCKYARE HGDVPCIADG 350
    GIQNSGHVMK ALALGANAVM MGSMLAGTEE APGEYYFHNG VRVKTYRGMG 400
    SLDAMRAGTR RTASPPARGL RSPEASPSTA ASSGGASRAS ALSEASPSAK 450
    SEASRTSTST GSAARYFAEN QTIRVAQGVS GCVVDKGTVM QLIPYVIQGV 500
    KHGMQDIGAR TLRDLHAQLV GGELRFDVRS GAAQREGDVH DLHSFERKLY 550
    A 551
    Length:551
    Mass (Da):59,047
    Last modified:July 5, 2005 - v1
    Checksum:i788A1DAC369E3DE9
    GO
    Isoform TgIMPDH-S (identifier: Q4VRV8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         361-551: ALALGANAVM...LHSFERKLYA → VWRCAEGRRCS

    Note: Lacks the active-site flap.

    Show »
    Length:371
    Mass (Da):40,366
    Checksum:i8376164171422C8F
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei361 – 551191ALALG…RKLYA → VWRCAEGRRCS in isoform TgIMPDH-S. 1 PublicationVSP_042319Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY663109 mRNA. Translation: AAV73841.1.
    AY661469 mRNA. Translation: AAV74388.1.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY663109 mRNA. Translation: AAV73841.1 .
    AY661469 mRNA. Translation: AAV74388.1 .

    3D structure databases

    ProteinModelPortali Q4VRV8.
    SMRi Q4VRV8. Positions 211-405.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BRENDAi 1.1.1.205. 262552.

    Family and domain databases

    Gene3Di 3.20.20.70. 2 hits.
    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. 2 hits.
    [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 [MRNA] (ISOFORMS TGIMPDH AND TGIMPDH-S), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, ENZYME REGULATION.
      Strain: RH.

    Entry informationi

    Entry nameiIMDH_TOXGO
    AccessioniPrimary (citable) accession number: Q4VRV8
    Secondary accession number(s): Q4VRV6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3