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Protein

UDP-glucose 4-epimerase

Gene

galE

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

Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD. It is only active on UDP-galactose and UDP-glucose.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

NAD+8 Publications

<p>This subsection of the ‘Function’ 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

Inhibited by UDP-phenol and NaBH3CN.2 Publications

<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

Kcat is 760 sec(-1) for UDP-Glc (at pH 8.5 and 27 degrees Celsius) and 24 sec(-1) for UDP-Gal (at pH 8.5).
  1. KM=18 µM for UDP-Gal (at pH 8.5)3 Publications
  2. KM=160 µM for UDP-Gal (at pH 8.5 and 27 degrees Celsius)3 Publications
  3. KM=225 µM for UDP-Glc (at pH 8.5 and 27 degrees Celsius)3 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: galactose metabolism

    This protein is involved in the pathway galactose metabolism, which is part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the pathway galactose metabolism and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei99NAD9 Publications1
    Binding sitei124NAD9 Publications1
    Binding sitei124Substrate1
    <p>This subsection of the ‘Function’ 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 sitei149Proton acceptor1 Publication1
    Binding sitei149NAD9 Publications1
    Binding sitei149Substrate1
    Binding sitei153NAD9 Publications1
    Binding sitei178NAD; via carbonyl oxygen9 Publications1
    Binding sitei179Substrate1
    Binding sitei231Substrate1
    Binding sitei299Substrate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi11 – 12NAD9 Publications2
    Nucleotide bindingi31 – 36NAD9 Publications6
    Nucleotide bindingi58 – 59NAD9 Publications2
    Nucleotide bindingi80 – 84NAD9 Publications5

    <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 functionIsomerase
    Biological processCarbohydrate metabolism, Galactose metabolism
    LigandNAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:UDPGLUCEPIM-MONOMER
    MetaCyc:UDPGLUCEPIM-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    5.1.3.2 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P09147

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

    More...
    UniPathwayi
    UPA00214

    <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_and_taxonomy_section">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:
    UDP-glucose 4-epimerase (EC:5.1.3.2)
    Alternative name(s):
    Galactowaldenase
    UDP-galactose 4-epimerase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:galE
    Synonyms:galD
    Ordered Locus Names:b0759, JW0742
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG10362 galE

    <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_and_biotech_section">'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>Mutagenesisi124S → A: No major structural changes. Catalytic efficiency is very low and affinity binding is 21% of the wild-type enzyme. 3 Publications1
    Mutagenesisi124S → T: No major structural changes. Catalytic efficiency is about 30% of that of the wild-type enzyme, and affinity binding is similar to that of the native enzyme. 3 Publications1
    Mutagenesisi149Y → F: No major structural changes. Catalytic efficiency is very low and affinity binding is 12% of the wild-type enzyme. 2 Publications1
    Mutagenesisi153K → A: Decreases the catalytic activity. Not reduced by sugars in the presence or absence of UMP. It contains very little NADH. 1 Publication1
    Mutagenesisi153K → M: Decreases the catalytic activity. Not reduced by sugars in the presence or absence of UMP. It contains very little NADH. 1 Publication1
    Mutagenesisi299Y → C: Loss of epimerase activity with UDP-Gal by almost 5-fold, but it results in a gain of epimerase activity with uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) by 230-fold with minimal changes in its three-dimensional structure. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB02790 Phenyl-Uridine-5'-Diphosphate
    DB01861 Uridine diphosphate glucose
    DB03435 Uridine-5'-Diphosphate
    DB04097 Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose
    DB02421 Uridine-5'-Diphosphate-Mannose
    DB03397 Uridine-Diphosphate-N-Acetylglucosamine

    <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_00001832031 – 338UDP-glucose 4-epimeraseAdd BLAST338

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P09147

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

    More...
    PaxDbi
    P09147

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P09147

    2D gel databases

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

    More...
    SWISS-2DPAGEi
    P09147

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By D-galactose and D-fucose.1 Publication

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.11 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4261900, 143 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-9728N

    Protein interaction database and analysis system

    More...
    IntActi
    P09147, 15 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_0827

    <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

    Secondary structure

    1338
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P09147

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

    More...
    SMRi
    P09147

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P09147

    <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

    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>Regioni199 – 200Substrate binding2
    Regioni216 – 218Substrate binding3
    Regioni292 – 295Substrate binding4

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CMR Bacteria
    COG1087 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000168001

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P09147

    KEGG Orthology (KO)

    More...
    KOi
    K01784

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P09147

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd05247 UDP_G4E_1_SDR_e, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR016040 NAD(P)-bd_dom
    IPR036291 NAD(P)-bd_dom_sf
    IPR005886 UDP_G4E

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF16363 GDP_Man_Dehyd, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01179 galE, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    P09147-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRVLVTGGSG YIGSHTCVQL LQNGHDVIIL DNLCNSKRSV LPVIERLGGK
    60 70 80 90 100
    HPTFVEGDIR NEALMTEILH DHAIDTVIHF AGLKAVGESV QKPLEYYDNN
    110 120 130 140 150
    VNGTLRLISA MRAANVKNFI FSSSATVYGD QPKIPYVESF PTGTPQSPYG
    160 170 180 190 200
    KSKLMVEQIL TDLQKAQPDW SIALLRYFNP VGAHPSGDMG EDPQGIPNNL
    210 220 230 240 250
    MPYIAQVAVG RRDSLAIFGN DYPTEDGTGV RDYIHVMDLA DGHVVAMEKL
    260 270 280 290 300
    ANKPGVHIYN LGAGVGNSVL DVVNAFSKAC GKPVNYHFAP RREGDLPAYW
    310 320 330
    ADASKADREL NWRVTRTLDE MAQDTWHWQS RHPQGYPD
    Length:338
    Mass (Da):37,265
    Last modified:July 1, 1989 - 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:i5CA8B4F7903F7792
    GO

    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 conflicti140 – 145FPTGTP → LLPIPG in CAA35813 (PubMed:2134186).Curated6

    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
    X06226 Genomic DNA Translation: CAA29573.1
    U00096 Genomic DNA Translation: AAC73846.1
    AP009048 Genomic DNA Translation: BAA35421.1
    X51449 Genomic DNA Translation: CAA35813.1
    U07867 Genomic DNA Translation: AAB06890.1
    J01613 Genomic DNA Translation: AAA87978.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S02089 XUECUG

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415280.3, NC_000913.3
    WP_001265438.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73846; AAC73846; b0759
    BAA35421; BAA35421; BAA35421

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    945354

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0742
    eco:b0759

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1519

    <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
    X06226 Genomic DNA Translation: CAA29573.1
    U00096 Genomic DNA Translation: AAC73846.1
    AP009048 Genomic DNA Translation: BAA35421.1
    X51449 Genomic DNA Translation: CAA35813.1
    U07867 Genomic DNA Translation: AAB06890.1
    J01613 Genomic DNA Translation: AAA87978.1
    PIRiS02089 XUECUG
    RefSeqiNP_415280.3, NC_000913.3
    WP_001265438.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1A9YX-ray1.80A1-338[»]
    1A9ZX-ray1.90A1-338[»]
    1KVQX-ray2.15A1-338[»]
    1KVRX-ray1.90A1-338[»]
    1KVSX-ray2.15A1-338[»]
    1KVTX-ray2.15A1-338[»]
    1KVUX-ray1.90A1-338[»]
    1LRJX-ray1.90A1-338[»]
    1LRKX-ray1.75A1-338[»]
    1LRLX-ray1.80A1-338[»]
    1NAHX-ray1.80A1-338[»]
    1NAIX-ray2.00A1-338[»]
    1UDAX-ray1.80A1-338[»]
    1UDBX-ray1.65A1-338[»]
    1UDCX-ray1.65A1-338[»]
    1XELX-ray1.80A1-338[»]
    2UDPX-ray1.80A/B1-338[»]
    5GY7X-ray1.43A/B1-338[»]
    ProteinModelPortaliP09147
    SMRiP09147
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261900, 143 interactors
    DIPiDIP-9728N
    IntActiP09147, 15 interactors
    STRINGi316385.ECDH10B_0827

    Chemistry databases

    DrugBankiDB02790 Phenyl-Uridine-5'-Diphosphate
    DB01861 Uridine diphosphate glucose
    DB03435 Uridine-5'-Diphosphate
    DB04097 Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose
    DB02421 Uridine-5'-Diphosphate-Mannose
    DB03397 Uridine-Diphosphate-N-Acetylglucosamine

    2D gel databases

    SWISS-2DPAGEiP09147

    Proteomic databases

    EPDiP09147
    PaxDbiP09147
    PRIDEiP09147

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73846; AAC73846; b0759
    BAA35421; BAA35421; BAA35421
    GeneIDi945354
    KEGGiecj:JW0742
    eco:b0759
    PATRICifig|1411691.4.peg.1519

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0357
    EcoGeneiEG10362 galE

    Phylogenomic databases

    eggNOGiENOG4105CMR Bacteria
    COG1087 LUCA
    HOGENOMiHOG000168001
    InParanoidiP09147
    KOiK01784
    PhylomeDBiP09147

    Enzyme and pathway databases

    UniPathwayi
    UPA00214

    BioCyciEcoCyc:UDPGLUCEPIM-MONOMER
    MetaCyc:UDPGLUCEPIM-MONOMER
    BRENDAi5.1.3.2 2026
    SABIO-RKiP09147

    Miscellaneous databases

    EvolutionaryTraceiP09147

    Protein Ontology

    More...
    PROi
    PR:P09147

    Family and domain databases

    CDDicd05247 UDP_G4E_1_SDR_e, 1 hit
    InterProiView protein in InterPro
    IPR016040 NAD(P)-bd_dom
    IPR036291 NAD(P)-bd_dom_sf
    IPR005886 UDP_G4E
    PfamiView protein in Pfam
    PF16363 GDP_Man_Dehyd, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR01179 galE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    <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 nameiGALE_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: P09147
    Secondary accession number(s): Q47493
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: December 5, 2018
    This is version 168 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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