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Q07152

- IMDH_DROME

UniProt

Q07152 - IMDH_DROME

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

ras

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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.2 PublicationsUniRule 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 bindingi345 – 3451Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi347 – 3471Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei348 – 3481IMPUniRule annotation
    Active sitei350 – 3501Thioimidate intermediateUniRule annotation
    Metal bindingi350 – 3501Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei464 – 4641IMPUniRule annotation
    Metal bindingi523 – 5231Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi524 – 5241Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi293 – 2953NADUniRule annotation
    Nucleotide bindingi343 – 3453NADUniRule 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. axon guidance Source: FlyBase
    2. GMP biosynthetic process Source: UniProtKB-HAMAP
    3. oogenesis Source: FlyBase
    4. phagocytosis Source: FlyBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    ReactomeiREACT_208157. 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
    Alternative name(s):
    Protein raspberry
    Gene namesi
    Name:ras
    ORF Names:CG1799
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0003204. ras.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 537537Inosine-5'-monophosphate dehydrogenasePRO_0000093678Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ07152.
    PRIDEiQ07152.

    Expressioni

    Tissue specificityi

    Enriched in adult ovary and testis.1 Publication

    Developmental stagei

    Expressed both maternally and zygotically.1 Publication

    Gene expression databases

    BgeeiQ07152.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    BioGridi68684. 9 interactions.
    DIPiDIP-21552N.
    IntActiQ07152. 4 interactions.
    MINTiMINT-910823.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07152.
    SMRiQ07152. Positions 38-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini136 – 19560CBS 1UniRule annotationAdd
    BLAST
    Domaini200 – 25657CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni383 – 3853IMP bindingUniRule annotation
    Regioni406 – 4072IMP bindingUniRule annotation
    Regioni430 – 4345IMP 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

    eggNOGiCOG0517.
    GeneTreeiENSGT00530000062923.
    InParanoidiQ07152.
    KOiK00088.
    OMAiFQAKARH.
    OrthoDBiEOG7VTDMM.
    PhylomeDBiQ07152.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q07152-1) [UniParc]FASTAAdd to Basket

    Also known as: C

    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

    MESTTKVKVN GFVESTSSSA APAIQTKSTT GFDAELQDGL SCKELFQNGE    50
    GLTYNDFLIL PGYIDFTAEE VDLSSPLTKS LTLRAPLVSS PMDTVTESEM 100
    AIAMALCGGI GIIHHNCTPE YQALEVHKVK KYKHGFMRDP SVMSPTNTVG 150
    DVLEARRKNG FTGYPVTENG KLGGKLLGMV TSRDIDFREN QPEVLLADIM 200
    TTELVTAPNG INLPTANAIL EKSKKGKLPI VNQAGELVAM IARTDLKKAR 250
    SYPNASKDSN KQLLVGAAIG TRSEDKARLA LLVANGVDVI ILDSSQGNSV 300
    YQVEMIKYIK ETYPELQVIG GNVVTRAQAK NLIDAGVDGL RVGMGSGSIC 350
    ITQEVMACGC PQATAVYQVS TYARQFGVPV IADGGIQSIG HIVKAIALGA 400
    SAVMMGSLLA GTSEAPGEYF FSDGVRLKKY RGMGSLEAME RGDAKGAAMS 450
    RYYHNEMDKM KVAQGVSGSI VDKGSVLRYL PYLECGLQHS CQDIGANSIN 500
    KLRDMIYNGQ LRFMKRTHSA QLEGNVHGLF SYEKRLF 537
    Length:537
    Mass (Da):57,829
    Last modified:November 1, 1995 - v1
    Checksum:iA5EAB41AEAA64EBD
    GO
    Isoform B (identifier: Q07152-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-91: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:446
    Mass (Da):48,139
    Checksum:i15746E0A799702BB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381D → V in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti53 – 531T → P in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti99 – 1024EMAI → RCH in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti184 – 1841D → A in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti194 – 1941V → S in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti216 – 2172AN → EH in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti226 – 2294GKLP → ATA in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti244 – 2441T → A in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti261 – 2622KQ → TR in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti265 – 2662VG → CP in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti277 – 2782AR → GCRA in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti284 – 2841A → R in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti301 – 3011Y → I in AAB35628. (PubMed:7476879)Curated
    Sequence conflicti387 – 3882QS → HA in AAB35628. (PubMed:7476879)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9191Missing in isoform B. 1 PublicationVSP_010299Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14847 Genomic DNA. Translation: AAA21831.1.
    L22608 mRNA. Translation: AAA16839.1.
    S80430 mRNA. Translation: AAB35628.1.
    AE014298 Genomic DNA. Translation: AAF46621.2.
    AE014298 Genomic DNA. Translation: AAF46622.1.
    AY089553 mRNA. Translation: AAL90291.1.
    PIRiS41064.
    S59508.
    RefSeqiNP_001259427.1. NM_001272498.1. [Q07152-1]
    NP_524646.4. NM_079907.6. [Q07152-2]
    NP_727441.1. NM_167240.2. [Q07152-1]
    NP_727442.1. NM_167241.2. [Q07152-1]
    UniGeneiDm.6459.

    Genome annotation databases

    EnsemblMetazoaiFBtr0071494; FBpp0071423; FBgn0003204. [Q07152-1]
    FBtr0071495; FBpp0071424; FBgn0003204. [Q07152-1]
    FBtr0332294; FBpp0304573; FBgn0003204. [Q07152-1]
    GeneIDi43873.
    KEGGidme:Dmel_CG1799.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14847 Genomic DNA. Translation: AAA21831.1 .
    L22608 mRNA. Translation: AAA16839.1 .
    S80430 mRNA. Translation: AAB35628.1 .
    AE014298 Genomic DNA. Translation: AAF46621.2 .
    AE014298 Genomic DNA. Translation: AAF46622.1 .
    AY089553 mRNA. Translation: AAL90291.1 .
    PIRi S41064.
    S59508.
    RefSeqi NP_001259427.1. NM_001272498.1. [Q07152-1 ]
    NP_524646.4. NM_079907.6. [Q07152-2 ]
    NP_727441.1. NM_167240.2. [Q07152-1 ]
    NP_727442.1. NM_167241.2. [Q07152-1 ]
    UniGenei Dm.6459.

    3D structure databases

    ProteinModelPortali Q07152.
    SMRi Q07152. Positions 38-537.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68684. 9 interactions.
    DIPi DIP-21552N.
    IntActi Q07152. 4 interactions.
    MINTi MINT-910823.

    Proteomic databases

    PaxDbi Q07152.
    PRIDEi Q07152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0071494 ; FBpp0071423 ; FBgn0003204 . [Q07152-1 ]
    FBtr0071495 ; FBpp0071424 ; FBgn0003204 . [Q07152-1 ]
    FBtr0332294 ; FBpp0304573 ; FBgn0003204 . [Q07152-1 ]
    GeneIDi 43873.
    KEGGi dme:Dmel_CG1799.

    Organism-specific databases

    CTDi 19412.
    FlyBasei FBgn0003204. ras.

    Phylogenomic databases

    eggNOGi COG0517.
    GeneTreei ENSGT00530000062923.
    InParanoidi Q07152.
    KOi K00088.
    OMAi FQAKARH.
    OrthoDBi EOG7VTDMM.
    PhylomeDBi Q07152.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    Reactomei REACT_208157. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    ChiTaRSi Ras85D. drosophila.
    GenomeRNAii 43873.
    NextBioi 836266.
    PROi Q07152.

    Gene expression databases

    Bgeei Q07152.

    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. "Drosophila inosine monophosphate dehydrogenase is encoded at the raspberry locus."
      Nash D., Hu S.
      (In) Proceedings of the 35th meeting of the Canadian Federation of Biological Societies, pp.72-72, Victoria (1992)
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM A).
      Strain: Oregon-R.
      Tissue: Embryo.
    2. "The raspberry locus of Drosophila melanogaster includes an inosine monophosphate dehydrogenase like coding sequence."
      Nash D., Hu S., Leonard N.J., Tiong S.Y., Fillips D.
      Genome 37:333-344(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION.
      Strain: Oregon-R.
      Tissue: Embryo.
    3. "Cloning and sequence analysis of a Drosophila melanogaster cDNA encoding IMP dehydrogenase."
      Sifri C.D., Wilson K., Smolik S., Forte M.A., Ullman B.
      Biochim. Biophys. Acta 1217:103-106(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
      Strain: Canton-S.
    4. "The raspberry locus encodes Drosophila inosine monophosphate dehydrogenase."
      Slee R., Bownes M.
      Mol. Gen. Genet. 248:755-766(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    5. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    6. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
      Strain: Berkeley.
      Tissue: Embryo.
    8. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiIMDH_DROME
    AccessioniPrimary (citable) accession number: Q07152
    Secondary accession number(s): Q26455, Q8SXM5, Q9W2R8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3