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Entry version 192 (22 Apr 2020)
Sequence version 1 (01 Oct 1996)
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Protein

Inosine-5'-monophosphate dehydrogenase 3

Gene

IMD3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 annotation3 Publications

Miscellaneous

Present with 26300 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

K+UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=100 µM for Inosine 5'-phosphate1 Publication
  2. KM=314 µM for NAD+1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: XMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Inosine-5'-monophosphate dehydrogenase 2 (IMD2), Inosine-5'-monophosphate dehydrogenase 3 (IMD3), Putative inosine-5'-monophosphate dehydrogenase 1 (IMD1), Inosine-5'-monophosphate dehydrogenase 4 (IMD4)
    This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi330Potassium; via carbonyl oxygenUniRule annotation1
    Metal bindingi332Potassium; via carbonyl oxygenUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei333IMPUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei335Thioimidate intermediateUniRule annotation1
    Metal bindingi335Potassium; via carbonyl oxygenUniRule annotation1
    Active sitei437Proton acceptorUniRule annotation1
    Binding sitei449IMPUniRule annotation1
    Metal bindingi508Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi509Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi510Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi278 – 280NADUniRule annotation3
    Nucleotide bindingi328 – 330NADUniRule annotation3

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    Biological processGMP biosynthesis, Purine biosynthesis
    LigandMetal-binding, NAD, Potassium

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:YLR432W-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-6798695 Neutrophil degranulation
    R-SCE-73817 Purine ribonucleoside monophosphate biosynthesis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P50095

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00601;UER00295

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenase 3UniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenase 3UniRule annotation
    Short name:
    IMPD 3UniRule annotation
    Short name:
    IMPDH 3UniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:IMD3UniRule annotation
    Ordered Locus Names:YLR432W
    ORF Names:L9753.4
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XII

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YLR432W

    Saccharomyces Genome Database

    More...
    SGDi
    S000004424 IMD3

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi253A → S: Increases drug-resistance to MPA. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000936831 – 523Inosine-5'-monophosphate dehydrogenase 3Add BLAST523

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P50095

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P50095

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P50095

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P50095

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer. Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4).

    UniRule annotation1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Show more details

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    31691, 180 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-1947N

    Protein interaction database and analysis system

    More...
    IntActi
    P50095, 199 interactors

    Molecular INTeraction database

    More...
    MINTi
    P50095

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YLR432W

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P50095 protein

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P50095

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini121 – 183CBS 1UniRule annotationAdd BLAST63
    Domaini184 – 240CBS 2UniRule annotationAdd BLAST57

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni368 – 370IMP bindingUniRule annotation3
    Regioni391 – 392IMP bindingUniRule annotation2
    Regioni415 – 419IMP bindingUniRule annotation5

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_022552_2_1_1

    KEGG Orthology (KO)

    More...
    KOi
    K00088

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    SSMGYCG

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00381 IMPDH, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.70, 2 hits

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01964 IMPDH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013785 Aldolase_TIM
    IPR000644 CBS_dom
    IPR005990 IMP_DH
    IPR015875 IMP_DH/GMP_Rdtase_CS
    IPR001093 IMP_DH_GMPRt

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00571 CBS, 2 hits
    PF00478 IMPDH, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000130 IMPDH, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00116 CBS, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01302 IMP_dehydrog, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51371 CBS, 2 hits
    PS00487 IMP_DH_GMP_RED, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P50095-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAAVRDYKTA LEFAKSLPRL DGLSVQELMD SKTRGGLTYN DFLVLPGLVD
    60 70 80 90 100
    FPSSEVSLQT KLTRNITLNT PFVSSPMDTV TESEMAIFMA LLGGIGFIHH
    110 120 130 140 150
    NCTPEDQADM VRRVKNYENG FINNPIVISP TTTVGEAKSM KERFGFSGFP
    160 170 180 190 200
    VTEDGKRNGK LMGIVTSRDI QFVEDNSLLV QDVMTKNPVT GAQGITLSEG
    210 220 230 240 250
    NEILKKIKKG KLLIVDDNGN LVSMLSRTDL MKNQNYPLAS KSATTKQLLC
    260 270 280 290 300
    GAAIGTIDAD KERLRLLVEA GLDVVILDSS QGNSIFQLNM IKWIKETFPD
    310 320 330 340 350
    LEIIAGNVAT REQAANLIAA GADGLRIGMG SGSICITQEV MACGRPQGTA
    360 370 380 390 400
    VYNVCEFANQ FGIPCMADGG VQNIGHITKA LALGSSTVMM GGMLAGTTES
    410 420 430 440 450
    PGEYFYQDGK RLKAYRGMGS IDAMQKTGTK GNASTSRYFS ESDSVLVAQG
    460 470 480 490 500
    VSGAVVDKGS IKKFIPYLYN GLQHSCQDIG YKSLTLLKEN VQSGKVRFEF
    510 520
    RTASAQLEGG VHNLHSYEKR LHN
    Length:523
    Mass (Da):56,585
    Last modified:October 1, 1996 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA0C84C22527AAEA6
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    U21094 Genomic DNA Translation: AAB67516.1
    BK006945 Genomic DNA Translation: DAA09733.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S59402

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_013536.3, NM_001182320.3

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YLR432W_mRNA; YLR432W; YLR432W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    851152

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YLR432W

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U21094 Genomic DNA Translation: AAB67516.1
    BK006945 Genomic DNA Translation: DAA09733.1
    PIRiS59402
    RefSeqiNP_013536.3, NM_001182320.3

    3D structure databases

    SMRiP50095
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi31691, 180 interactors
    DIPiDIP-1947N
    IntActiP50095, 199 interactors
    MINTiP50095
    STRINGi4932.YLR432W

    PTM databases

    iPTMnetiP50095

    Proteomic databases

    MaxQBiP50095
    PaxDbiP50095
    PRIDEiP50095

    Genome annotation databases

    EnsemblFungiiYLR432W_mRNA; YLR432W; YLR432W
    GeneIDi851152
    KEGGisce:YLR432W

    Organism-specific databases

    EuPathDBiFungiDB:YLR432W
    SGDiS000004424 IMD3

    Phylogenomic databases

    HOGENOMiCLU_022552_2_1_1
    KOiK00088
    OMAiSSMGYCG

    Enzyme and pathway databases

    UniPathwayiUPA00601;UER00295
    BioCyciYEAST:YLR432W-MONOMER
    ReactomeiR-SCE-6798695 Neutrophil degranulation
    R-SCE-73817 Purine ribonucleoside monophosphate biosynthesis
    SABIO-RKiP50095

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P50095
    RNActiP50095 protein

    Family and domain databases

    CDDicd00381 IMPDH, 1 hit
    Gene3Di3.20.20.70, 2 hits
    HAMAPiMF_01964 IMPDH, 1 hit
    InterProiView protein in InterPro
    IPR013785 Aldolase_TIM
    IPR000644 CBS_dom
    IPR005990 IMP_DH
    IPR015875 IMP_DH/GMP_Rdtase_CS
    IPR001093 IMP_DH_GMPRt
    PfamiView protein in Pfam
    PF00571 CBS, 2 hits
    PF00478 IMPDH, 1 hit
    PIRSFiPIRSF000130 IMPDH, 1 hit
    SMARTiView protein in SMART
    SM00116 CBS, 2 hits
    TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
    PROSITEiView protein in PROSITE
    PS51371 CBS, 2 hits
    PS00487 IMP_DH_GMP_RED, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIMDH3_YEAST
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P50095
    Secondary accession number(s): D6VZ67
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: April 22, 2020
    This is version 192 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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