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Entry version 124 (26 Feb 2020)
Sequence version 1 (06 Dec 2005)
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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Escherichia coli (strain K12)
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 annotation1 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. IMP dehydrogenase subunit of E.coli contains a cysteine at the IMP binding site and is inhibited in a simple competitive manner by GMP. It does not exhibit allosteric properties as does IMP dehydrogenase from B.subtilis or S.typhimurium.UniRule annotation1 Publication

<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=61 µM for Inosine 5'-phosphate1 Publication
  2. KM=2000 µM for NAD+1 Publication
  3. KM=2.8 mM for K+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 (guaB)
    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 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 sitei248NADUniRule annotation1
    <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 bindingi300Potassium; via carbonyl oxygenUniRule annotation1
    Metal bindingi302Potassium; via carbonyl oxygenUniRule annotation1
    Binding sitei303IMPUniRule 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 sitei305Thioimidate intermediateUniRule annotation1
    Metal bindingi305Potassium; via carbonyl oxygenUniRule annotation1
    Active sitei401Proton acceptorUniRule annotation1
    Binding sitei415IMPUniRule annotation1
    Metal bindingi469Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi470Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi471Potassium; 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 bindingi248 – 250NADUniRule annotation3
    Nucleotide bindingi298 – 300NADUniRule 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
    EcoCyc:IMP-DEHYDROG-MONOMER
    ECOL316407:JW5401-MONOMER
    MetaCyc:IMP-DEHYDROG-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0ADG7

    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 dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenaseUniRule annotation
    Short name:
    IMPDUniRule annotation
    Short name:
    IMPDHUniRule 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:guaBUniRule annotation
    Synonyms:guaR
    Ordered Locus Names:b2508, JW5401
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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
    • UP000000318 <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
    • UP000000625 Componenti: Chromosome

    <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

    GO - Cellular componenti

    <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>Mutagenesisi13D → A: Causes a 38-fold increase in the value of Km for K(+). No change is observed in the value of Km for IMP. 1 Publication1
    Mutagenesisi50D → A: Causes a 17-fold increase in the value of Km for K(+). 1 Publication1
    Mutagenesisi54E → A: No effect. 1 Publication1
    Mutagenesisi138D → A: No effect. 1 Publication1
    Mutagenesisi200D → A: No effect. 1 Publication1
    Mutagenesisi243D → A: No effect. 1 Publication1
    Mutagenesisi248D → A: Causes a 130-fold decrease in the value of kcat. 1 Publication1
    Mutagenesisi338D → A: Decreases the value of kcat by 600-fold. Increases the value of Km for IMP by 12-fold. 1 Publication1
    Mutagenesisi369E → A: No effect. 1 Publication1
    Mutagenesisi373E → A: No effect. 1 Publication1
    Mutagenesisi469E → A: Increases the value of Km for K(+) by 17-fold. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3630

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000936951 – 488Inosine-5'-monophosphate dehydrogenaseAdd BLAST488

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei267N6-acetyllysine1 Publication1
    Modified residuei428N6-acetyllysine1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0ADG7

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0ADG7

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

    More...
    PaxDbi
    P0ADG7

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0ADG7

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P0ADG7

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P0ADG7

    <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.

    UniRule annotation1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4263221, 88 interactors
    851324, 1 interactor

    Database of interacting proteins

    More...
    DIPi
    DIP-36207N

    Protein interaction database and analysis system

    More...
    IntActi
    P0ADG7, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2508

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P0ADG7

    <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
    P0ADG7

    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>Domaini93 – 149CBS 1UniRule annotationAdd BLAST57
    Domaini153 – 214CBS 2UniRule annotationAdd BLAST62

    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>Regioni338 – 340IMP bindingUniRule annotation3
    Regioni361 – 362IMP bindingUniRule annotation2
    Regioni385 – 389IMP bindingUniRule annotation5

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The CBS domain of IMPDH is a negative trans-regulator of adenylate nucleotide synthesis, and this role is independent of the catalytic function of IMPDH in the de novo GMP biosynthesis. Deletion of the CBS domain derepresses the synthesis of AMP from IMP.2 Publications

    <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

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CP4 Bacteria
    COG0516 LUCA
    COG0517 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_022552_2_2_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0ADG7

    KEGG Orthology (KO)

    More...
    KOi
    K00088

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0ADG7

    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, 1 hit

    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.

    P0ADG7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLRIAKEALT FDDVLLVPAH STVLPNTADL STQLTKTIRL NIPMLSAAMD
    60 70 80 90 100
    TVTEARLAIA LAQEGGIGFI HKNMSIERQA EEVRRVKKHE SGVVTDPQTV
    110 120 130 140 150
    LPTTTLREVK ELTERNGFAG YPVVTEENEL VGIITGRDVR FVTDLNQPVS
    160 170 180 190 200
    VYMTPKERLV TVREGEAREV VLAKMHEKRV EKALVVDDEF HLIGMITVKD
    210 220 230 240 250
    FQKAERKPNA CKDEQGRLRV GAAVGAGAGN EERVDALVAA GVDVLLIDSS
    260 270 280 290 300
    HGHSEGVLQR IRETRAKYPD LQIIGGNVAT AAGARALAEA GCSAVKVGIG
    310 320 330 340 350
    PGSICTTRIV TGVGVPQITA VADAVEALEG TGIPVIADGG IRFSGDIAKA
    360 370 380 390 400
    IAAGASAVMV GSMLAGTEES PGEIELYQGR SYKSYRGMGS LGAMSKGSSD
    410 420 430 440 450
    RYFQSDNAAD KLVPEGIEGR VAYKGRLKEI IHQQMGGLRS CMGLTGCGTI
    460 470 480
    DELRTKAEFV RISGAGIQES HVHDVTITKE SPNYRLGS
    Length:488
    Mass (Da):52,022
    Last modified:December 6, 2005 - 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:iB0FD0A786779C98E
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence CAA26133 differs from that shown. Reason: Erroneous initiation.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti206R → A in CAA26133 (PubMed:2860637).Curated1
    Sequence conflicti206R → A in AAB18618 (PubMed:2860637).Curated1

    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
    X02209 Genomic DNA Translation: CAA26133.1 Different initiation.
    U00096 Genomic DNA Translation: AAC75561.1
    AP009048 Genomic DNA Translation: BAA16395.2
    M10101 Genomic DNA Translation: AAB18618.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    C65027 DEECIP

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417003.1, NC_000913.3
    WP_001299507.1, NZ_STEB01000011.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75561; AAC75561; b2508
    BAA16395; BAA16395; BAA16395

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946985

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW5401
    eco:b2508

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4229

    <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
    X02209 Genomic DNA Translation: CAA26133.1 Different initiation.
    U00096 Genomic DNA Translation: AAC75561.1
    AP009048 Genomic DNA Translation: BAA16395.2
    M10101 Genomic DNA Translation: AAB18618.1
    PIRiC65027 DEECIP
    RefSeqiNP_417003.1, NC_000913.3
    WP_001299507.1, NZ_STEB01000011.1

    3D structure databases

    SMRiP0ADG7
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4263221, 88 interactors
    851324, 1 interactor
    DIPiDIP-36207N
    IntActiP0ADG7, 1 interactor
    STRINGi511145.b2508

    Chemistry databases

    BindingDBiP0ADG7
    ChEMBLiCHEMBL3630

    PTM databases

    iPTMnetiP0ADG7

    2D gel databases

    SWISS-2DPAGEiP0ADG7

    Proteomic databases

    EPDiP0ADG7
    jPOSTiP0ADG7
    PaxDbiP0ADG7
    PRIDEiP0ADG7

    Genome annotation databases

    EnsemblBacteriaiAAC75561; AAC75561; b2508
    BAA16395; BAA16395; BAA16395
    GeneIDi946985
    KEGGiecj:JW5401
    eco:b2508
    PATRICifig|1411691.4.peg.4229

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0416

    Phylogenomic databases

    eggNOGiENOG4105CP4 Bacteria
    COG0516 LUCA
    COG0517 LUCA
    HOGENOMiCLU_022552_2_2_6
    InParanoidiP0ADG7
    KOiK00088
    PhylomeDBiP0ADG7

    Enzyme and pathway databases

    UniPathwayiUPA00601;UER00295
    BioCyciEcoCyc:IMP-DEHYDROG-MONOMER
    ECOL316407:JW5401-MONOMER
    MetaCyc:IMP-DEHYDROG-MONOMER
    SABIO-RKiP0ADG7

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P0ADG7

    Family and domain databases

    CDDicd00381 IMPDH, 1 hit
    Gene3Di3.20.20.70, 1 hit
    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 nameiIMDH_ECOLI
    <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: P0ADG7
    Secondary accession number(s): P06981, P76574, P78202
    <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: April 1, 1988
    Last sequence update: December 6, 2005
    Last modified: February 26, 2020
    This is version 124 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 programProkaryotic 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

    Direct protein sequencing, Reference proteome

    Documents

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