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O14344

- IMDH_SCHPO

UniProt

O14344 - IMDH_SCHPO

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

gua1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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
    Metal bindingi332 – 3321Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi334 – 3341Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei335 – 3351IMPUniRule annotation
    Active sitei337 – 3371Thioimidate intermediateUniRule annotation
    Metal bindingi337 – 3371Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei451 – 4511IMPUniRule annotation
    Metal bindingi510 – 5101Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi511 – 5111Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi280 – 2823NADUniRule annotation
    Nucleotide bindingi330 – 3323NADUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP
    2. GTP biosynthetic process Source: PomBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    ReactomeiREACT_207552. Purine ribonucleoside monophosphate biosynthesis.
    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:gua1
    ORF Names:SPBC2F12.14c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC2F12.14c.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytosol Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 524524Inosine-5'-monophosphate dehydrogenasePRO_0000093680Add
    BLAST

    Proteomic databases

    MaxQBiO14344.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    BioGridi276845. 6 interactions.
    MINTiMINT-4672477.
    STRINGi4896.SPBC2F12.14c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO14344.
    SMRiO14344. Positions 17-118.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini121 – 18060CBS 1UniRule annotationAdd
    BLAST
    Domaini184 – 24259CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni370 – 3723IMP bindingUniRule annotation
    Regioni393 – 3942IMP bindingUniRule annotation
    Regioni417 – 4215IMP bindingUniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    HOGENOMiHOG000165752.
    KOiK00088.
    OMAiNNSQKRY.
    PhylomeDBiO14344.

    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.

    O14344-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAFKPYTEA LEVLKKYEKK DGLSIDDLIR HNFQGGLTFN DFLILPGYID    50
    FVPNNVSLET RISRNIVLKT PFMSSPMDTV TEDQMAIYMA LLGGIGVIHH 100
    NCTPEEQAAM VRKVKKYENG FILDPVVFSP QHTVGDVLKI KETKGFSGIP 150
    ITENGKLRGK LVGIVTSRDV QFHKDTNTPV TEVMTPREEL ITTAEGISLE 200
    RANEMLRKSK KGKLPVVDKD DNLVALLSLT DLMKNLHFPL ASKTSDTKQL 250
    MVAAAIGTRD DDRTRLALLA EAGLDAVVID SSQGNSCFQI EMIKWIKKTY 300
    PKIDVIAGNV VTREQTASLI AAGADGLRVG MGSGSACITQ EVMACGRPQA 350
    TAIAQVAEFA SQFGIGVIAD GGIQNVGHMV KSLSLGATAV MMGGLLAGTT 400
    ESPGEYYVRE GQRYKSYRGM GSIAAMEGTG VNKNASTGRY FSENDAVRVA 450
    QGVSGLVVDK GSLLRFLPYL YTGLQHALQD IGTKSLDELH EAVDKHEVRF 500
    ELRSSAAIRE GDIQGFATYE KRLY 524
    Length:524
    Mass (Da):57,026
    Last modified:January 1, 1998 - v1
    Checksum:iE6C822C22E74674F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti253 – 2531A → G in BAA13769. (PubMed:9501991)Curated
    Sequence conflicti263 – 2631R → P in BAA13769. (PubMed:9501991)Curated
    Sequence conflicti508 – 5092IR → TRK in CAB97003. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB10161.1.
    D89106 mRNA. Translation: BAA13769.1.
    AJ293460 Genomic DNA. Translation: CAB97003.1.
    PIRiT40127.
    RefSeqiNP_595702.1. NM_001021599.2.

    Genome annotation databases

    EnsemblFungiiSPBC2F12.14c.1; SPBC2F12.14c.1:pep; SPBC2F12.14c.
    GeneIDi2540315.
    KEGGispo:SPBC2F12.14c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB10161.1 .
    D89106 mRNA. Translation: BAA13769.1 .
    AJ293460 Genomic DNA. Translation: CAB97003.1 .
    PIRi T40127.
    RefSeqi NP_595702.1. NM_001021599.2.

    3D structure databases

    ProteinModelPortali O14344.
    SMRi O14344. Positions 17-118.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276845. 6 interactions.
    MINTi MINT-4672477.
    STRINGi 4896.SPBC2F12.14c-1.

    Proteomic databases

    MaxQBi O14344.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC2F12.14c.1 ; SPBC2F12.14c.1:pep ; SPBC2F12.14c .
    GeneIDi 2540315.
    KEGGi spo:SPBC2F12.14c.

    Organism-specific databases

    PomBasei SPBC2F12.14c.

    Phylogenomic databases

    HOGENOMi HOG000165752.
    KOi K00088.
    OMAi NNSQKRY.
    PhylomeDBi O14344.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    Reactomei REACT_207552. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    NextBioi 20801444.
    PROi O14344.

    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. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
      Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
      DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-293.
      Strain: PR745.
    3. Karaer S., Topal Sarykaya A., Temizkan G.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 378-524.
      Strain: 972 / ATCC 24843.
    4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
      Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
      Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIMDH_SCHPO
    AccessioniPrimary (citable) accession number: O14344
    Secondary accession number(s): P78758, Q9P3X8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3