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Entry version 147 (13 Nov 2019)
Sequence version 1 (01 Feb 1995)
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Protein

3-keto-L-gulonate-6-phosphate decarboxylase UlaD

Gene

ulaD

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 decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization.1 Publication

Miscellaneous

The reaction mechanism proceeds via the formation of a Mg2+ ion-stabilized 1,2-cis-enediolate intermediate. Water molecules competitively shuttle protons from the side chains of His-136 and Arg-139 to alternate faces of this intermediate. The active site is located at the interface of the component polypeptides.

<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

Mg2+Note: Binds 1 Mg2+ ion per subunit.

<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=0.67 mM for 3-keto-L-gulonate-6-P1 Publication

    <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: L-ascorbate degradation

    This protein is involved in step 2 of the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Probable L-ascorbate-6-phosphate lactonase UlaG (ulaG), Probable L-ascorbate-6-phosphate lactonase UlaG (ulaG), Probable L-ascorbate-6-phosphate lactonase UlaG (ulaG)
    2. 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD), 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD), 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD)
    3. L-ribulose-5-phosphate 3-epimerase UlaE (ulaE), L-ribulose-5-phosphate 3-epimerase UlaE (ulaE), L-ribulose-5-phosphate 3-epimerase UlaE (ulaE), L-ribulose-5-phosphate 3-epimerase UlaE (ulaE)
    4. L-ribulose-5-phosphate 4-epimerase UlaF (ulaF), L-ribulose-5-phosphate 4-epimerase UlaF (ulaF), L-ribulose-5-phosphate 4-epimerase UlaF (ulaF), L-ribulose-5-phosphate 4-epimerase UlaF (ulaF)
    This subpathway is part of the pathway L-ascorbate degradation, which is itself part of Cofactor degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate, the pathway L-ascorbate degradation and in Cofactor degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei11Substrate1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi33Magnesium1
    Metal bindingi62Magnesium1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei64Transition state stabilizer1
    Sitei67Transition state stabilizer1
    Binding sitei192Substrate1

    <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 functionDecarboxylase, Lyase
    Biological processCarbohydrate metabolism
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G7858-MONOMER
    ECOL316407:JW4154-MONOMER
    MetaCyc:G7858-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.1.85 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P39304

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

    More...
    UniPathwayi
    UPA00263;UER00378

    <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:
    3-keto-L-gulonate-6-phosphate decarboxylase UlaD (EC:4.1.1.85)
    Alternative name(s):
    3-dehydro-L-gulonate-6-phosphate decarboxylase
    KGPDC
    L-ascorbate utilization protein D
    <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:ulaD
    Synonyms:sgaH, yjfV
    Ordered Locus Names:b4196, JW4154
    <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

    <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>Mutagenesisi33E → K: Loss of activity. 1 Publication1
    Mutagenesisi64K → A: 16% of wild-type activity. 1 Publication1
    Mutagenesisi67D → A: 5% of wild-type activity. 1 Publication1
    Mutagenesisi112E → A: 0.5% of wild-type activity. 1 Publication1
    Mutagenesisi136H → A: 5% of wild-type activity. 1 Publication1
    Mutagenesisi139R → V: 17% of wild-type activity. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB01655 L-gulonic acid 6-phosphate
    DB03855 L-Threonohydroxamate 4-Phosphate
    DB02630 L-xylitol 5-phosphate
    DB01923 L-Xylulose 5-Phosphate
    DB04034 Ribulose-5-Phosphate

    <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_00002121031 – 2163-keto-L-gulonate-6-phosphate decarboxylase UlaDAdd BLAST216

    Proteomic databases

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

    More...
    PaxDbi
    P39304

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P39304

    2D gel databases

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

    More...
    SWISS-2DPAGEi
    P39304

    <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

    Induced by L-ascorbate. Repressed by UlaR.2 Publications

    <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.

    3 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4262000, 15 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10869N

    Protein interaction database and analysis system

    More...
    IntActi
    P39304, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b4196

    <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

    1216
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    P39304

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P39304

    <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

    <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 HPS/KGPDC family. KGPDC subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105H6Q Bacteria
    COG0269 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000226068

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P39304

    KEGG Orthology (KO)

    More...
    KOi
    K03078

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P39304

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd04726 KGPDC_HPS, 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_01267 UlaD, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR023942 3-keto-L-gulonate6Pdecase_UlaD
    IPR013785 Aldolase_TIM
    IPR041710 HPS/KGPDC
    IPR001754 OMPdeCOase_dom
    IPR011060 RibuloseP-bd_barrel

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00215 OMPdecase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00934 OMPdecase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51366 SSF51366, 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>. 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_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.

    P39304-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSLPMLQVAL DNQTMDSAYE TTRLIAEEVD IIEVGTILCV GEGVRAVRDL
    60 70 80 90 100
    KALYPHKIVL ADAKIADAGK ILSRMCFEAN ADWVTVICCA DINTAKGALD
    110 120 130 140 150
    VAKEFNGDVQ IELTGYWTWE QAQQWRDAGI GQVVYHRSRD AQAAGVAWGE
    160 170 180 190 200
    ADITAIKRLS DMGFKVTVTG GLALEDLPLF KGIPIHVFIA GRSIRDAASP
    210
    VEAARQFKRS IAELWG
    Length:216
    Mass (Da):23,578
    Last modified:February 1, 1995 - 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:iEC8490DA1D02D824
    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
    U14003 Genomic DNA Translation: AAA97092.1
    U00096 Genomic DNA Translation: AAC77153.1
    AP009048 Genomic DNA Translation: BAE78197.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S56421

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418617.1, NC_000913.3
    WP_000056749.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC77153; AAC77153; b4196
    BAE78197; BAE78197; BAE78197

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948714

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW4154
    eco:b4196

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2505

    <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
    U14003 Genomic DNA Translation: AAA97092.1
    U00096 Genomic DNA Translation: AAC77153.1
    AP009048 Genomic DNA Translation: BAE78197.1
    PIRiS56421
    RefSeqiNP_418617.1, NC_000913.3
    WP_000056749.1, 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
    1KV8X-ray1.62A/B1-216[»]
    1KW1X-ray2.20A/B1-216[»]
    1Q6LX-ray1.80A/B1-216[»]
    1Q6OX-ray1.20A/B1-216[»]
    1Q6QX-ray1.70A/B1-216[»]
    1Q6RX-ray1.76A/B1-216[»]
    1SO3X-ray1.90A/B1-216[»]
    1SO4X-ray1.70A/B1-216[»]
    1SO5X-ray1.80A/B1-216[»]
    1SO6X-ray1.90A/B1-216[»]
    1XBVX-ray1.66A/B1-216[»]
    1XBXX-ray1.81A/B1-216[»]
    1XBYX-ray1.58A/B1-216[»]
    1XBZX-ray1.80A/B1-216[»]
    SMRiP39304
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4262000, 15 interactors
    DIPiDIP-10869N
    IntActiP39304, 1 interactor
    STRINGi511145.b4196

    Chemistry databases

    DrugBankiDB01655 L-gulonic acid 6-phosphate
    DB03855 L-Threonohydroxamate 4-Phosphate
    DB02630 L-xylitol 5-phosphate
    DB01923 L-Xylulose 5-Phosphate
    DB04034 Ribulose-5-Phosphate

    2D gel databases

    SWISS-2DPAGEiP39304

    Proteomic databases

    PaxDbiP39304
    PRIDEiP39304

    Genome annotation databases

    EnsemblBacteriaiAAC77153; AAC77153; b4196
    BAE78197; BAE78197; BAE78197
    GeneIDi948714
    KEGGiecj:JW4154
    eco:b4196
    PATRICifig|1411691.4.peg.2505

    Organism-specific databases

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

    More...
    EchoBASEi
    EB2389

    Phylogenomic databases

    eggNOGiENOG4105H6Q Bacteria
    COG0269 LUCA
    HOGENOMiHOG000226068
    InParanoidiP39304
    KOiK03078
    PhylomeDBiP39304

    Enzyme and pathway databases

    UniPathwayiUPA00263;UER00378
    BioCyciEcoCyc:G7858-MONOMER
    ECOL316407:JW4154-MONOMER
    MetaCyc:G7858-MONOMER
    BRENDAi4.1.1.85 2026
    SABIO-RKiP39304

    Miscellaneous databases

    EvolutionaryTraceiP39304

    Protein Ontology

    More...
    PROi
    PR:P39304

    Family and domain databases

    CDDicd04726 KGPDC_HPS, 1 hit
    Gene3Di3.20.20.70, 1 hit
    HAMAPiMF_01267 UlaD, 1 hit
    InterProiView protein in InterPro
    IPR023942 3-keto-L-gulonate6Pdecase_UlaD
    IPR013785 Aldolase_TIM
    IPR041710 HPS/KGPDC
    IPR001754 OMPdeCOase_dom
    IPR011060 RibuloseP-bd_barrel
    PfamiView protein in Pfam
    PF00215 OMPdecase, 1 hit
    SMARTiView protein in SMART
    SM00934 OMPdecase, 1 hit
    SUPFAMiSSF51366 SSF51366, 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 nameiULAD_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: P39304
    Secondary accession number(s): Q2M6A9
    <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: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: November 13, 2019
    This is version 147 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. SIMILARITY comments
      Index of protein domains and families
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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