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Entry version 151 (18 Sep 2019)
Sequence version 1 (01 Dec 1992)
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Protein

dCTP deaminase

Gene

dcd

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 deamination of dCTP to dUTP.UniRule annotation4 Publications

<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 <a href="http://www.uniprot.org/help/function_section">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

Inhibited by dTTP, which binds to the active site and stabilizes the inactive form of the enzyme (PubMed:17651436). Inhibited by inorganic phosphate (PubMed:15539408).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 1.24 sec(-1).1 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: dUMP biosynthesis

      This protein is involved in step 1 of the subpathway that synthesizes dUMP from dCTP (dUTP route).UniRule annotation1 Publication
      Proteins known to be involved in the 2 steps of the subpathway in this organism are:
      1. dCTP deaminase (dcd), dCTP deaminase (dcd), dCTP deaminase (dcd), dCTP deaminase (dcd)
      2. Deoxyuridine 5'-triphosphate nucleotidohydrolase (dut), Deoxyuridine 5'-triphosphate nucleotidohydrolase (dut)
      This subpathway is part of the pathway dUMP biosynthesis, which is itself part of Pyrimidine metabolism.
      View all proteins of this organism that are known to be involved in the subpathway that synthesizes dUMP from dCTP (dUTP route), the pathway dUMP biosynthesis and in Pyrimidine metabolism.

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei138Proton donor/acceptorUniRule annotation2 Publications1
      <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 sitei178dCTPUniRule annotation2 Publications1
      Binding sitei182dCTPUniRule annotation2 Publications1

      Regions

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi110 – 115dCTP bindingUniRule annotation3 Publications6
      Nucleotide bindingi124 – 128dCTP binding3 Publications5
      Nucleotide bindingi136 – 138dCTP bindingUniRule annotation3 Publications3
      Nucleotide bindingi171 – 174dCTP binding2 Publications4

      <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

      • dCTP deaminase activity Source: EcoCyc
      • nucleotide binding Source: UniProtKB-KW

      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 functionHydrolase
      Biological processNucleotide metabolism
      LigandNucleotide-binding

      Enzyme and pathway databases

      BioCyc Collection of Pathway/Genome Databases

      More...
      BioCyci
      EcoCyc:DCTP-DEAM-MONOMER
      ECOL316407:JW2050-MONOMER
      MetaCyc:DCTP-DEAM-MONOMER

      BRENDA Comprehensive Enzyme Information System

      More...
      BRENDAi
      3.5.4.13 2026

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

      More...
      UniPathwayi
      UPA00610;UER00665

      <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:
      dCTP deaminase1 PublicationUniRule annotation (EC:3.5.4.13UniRule annotation1 Publication)
      Alternative name(s):
      Deoxycytidine triphosphate deaminaseUniRule annotation
      <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:dcd1 PublicationUniRule annotation
      Synonyms:dus1 Publication, paxA
      Ordered Locus Names:b2065, JW2050
      <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
      EG11418 dcd

      <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

      <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

      Mutant accumulates dCTP.1 Publication

      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>Mutagenesisi111S → C: Loss of activity. 1 Publication1
      Mutagenesisi111S → T: 30-fold decrease in kcat. Shows altered dTTP inhibition. 1 Publication1
      Mutagenesisi115R → A: Loss of activity. 1 Publication1
      Mutagenesisi115R → Q: Loss of activity. 1 Publication1
      Mutagenesisi121H → A: Loss of activity. 1 Publication1
      Mutagenesisi122V → G: Loss of activity. 1 Publication1
      Mutagenesisi138E → A or Q: Loss of activity. 1 Publication1
      Mutagenesisi138E → D: 140-fold decrease in kcat. Shows altered dTTP inhibition. 1 Publication1

      Chemistry databases

      Drug and drug target database

      More...
      DrugBanki
      DB03258 2'-Deoxycytidine 5'-triphosphate
      DB02333 Deoxyuridine-5'-Triphosphate

      <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_00001559841 – 193dCTP deaminaseAdd BLAST193

      Proteomic databases

      jPOST - Japan Proteome Standard Repository/Database

      More...
      jPOSTi
      P28248

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

      More...
      PaxDbi
      P28248

      PRoteomics IDEntifications database

      More...
      PRIDEi
      P28248

      <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

      Homotrimer.

      UniRule annotation3 Publications

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGrid)

      More...
      BioGridi
      4259684, 5 interactors

      Protein interaction database and analysis system

      More...
      IntActi
      P28248, 2 interactors

      STRING: functional protein association networks

      More...
      STRINGi
      511145.b2065

      <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

      1193
      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
      P28248

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      Miscellaneous databases

      Relative evolutionary importance of amino acids within a protein sequence

      More...
      EvolutionaryTracei
      P28248

      <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 dCTP deaminase family.UniRule annotationCurated

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      ENOG4105DHP Bacteria
      COG0717 LUCA

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...
      HOGENOMi
      HOG000228601

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      P28248

      KEGG Orthology (KO)

      More...
      KOi
      K01494

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      P28248

      Family and domain databases

      Conserved Domains Database

      More...
      CDDi
      cd07557 trimeric_dUTPase, 1 hit

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      2.70.40.10, 1 hit

      HAMAP database of protein families

      More...
      HAMAPi
      MF_00146 dCTP_deaminase, 1 hit

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR011962 dCTP_deaminase
      IPR029054 dUTPase-like
      IPR036157 dUTPase-like_sf
      IPR033704 dUTPase_trimeric

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF00692 dUTPase, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF51283 SSF51283, 1 hit

      TIGRFAMs; a protein family database

      More...
      TIGRFAMsi
      TIGR02274 dCTP_deam, 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.

      P28248-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MRLCDRDIEA WLDEGRLSIN PRPPVERING ATVDVRLGNK FRTFRGHTAA
      60 70 80 90 100
      FIDLSGPKDE VSAALDRVMS DEIVLDEGEA FYLHPGELAL AVTLESVTLP
      110 120 130 140 150
      ADLVGWLDGR SSLARLGLMV HVTAHRIDPG WSGCIVLEFY NSGKLPLALR
      160 170 180 190
      PGMLIGALSF EPLSGPAVRP YNRREDAKYR NQQGAVASRI DKD
      Length:193
      Mass (Da):21,249
      Last modified:December 1, 1992 - 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:iB0044051ADE7F919
      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
      M90069 Genomic DNA Translation: AAA23669.1
      U00096 Genomic DNA Translation: AAC75126.1
      AP009048 Genomic DNA Translation: BAA15918.1

      Protein sequence database of the Protein Information Resource

      More...
      PIRi
      A42940

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_416569.1, NC_000913.3
      WP_001234768.1, NZ_LN832404.1

      Genome annotation databases

      Ensembl bacterial and archaeal genome annotation project

      More...
      EnsemblBacteriai
      AAC75126; AAC75126; b2065
      BAA15918; BAA15918; BAA15918

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      946593

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      ecj:JW2050
      eco:b2065

      Pathosystems Resource Integration Center (PATRIC)

      More...
      PATRICi
      fig|1411691.4.peg.186

      <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
      M90069 Genomic DNA Translation: AAA23669.1
      U00096 Genomic DNA Translation: AAC75126.1
      AP009048 Genomic DNA Translation: BAA15918.1
      PIRiA42940
      RefSeqiNP_416569.1, NC_000913.3
      WP_001234768.1, 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
      1XS1X-ray1.80A/B/C/D/E/F1-193[»]
      1XS4X-ray2.53A/B/C/D/E/F1-193[»]
      1XS6X-ray2.00A/B/C/D/E/F1-193[»]
      2J4HX-ray2.70A/B1-193[»]
      2J4QX-ray2.60A/B1-193[»]
      2V9XX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-193[»]
      SMRiP28248
      ModBaseiSearch...

      Protein-protein interaction databases

      BioGridi4259684, 5 interactors
      IntActiP28248, 2 interactors
      STRINGi511145.b2065

      Chemistry databases

      DrugBankiDB03258 2'-Deoxycytidine 5'-triphosphate
      DB02333 Deoxyuridine-5'-Triphosphate

      Proteomic databases

      jPOSTiP28248
      PaxDbiP28248
      PRIDEiP28248

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsemblBacteriaiAAC75126; AAC75126; b2065
      BAA15918; BAA15918; BAA15918
      GeneIDi946593
      KEGGiecj:JW2050
      eco:b2065
      PATRICifig|1411691.4.peg.186

      Organism-specific databases

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

      More...
      EchoBASEi
      EB1389
      EcoGeneiEG11418 dcd

      Phylogenomic databases

      eggNOGiENOG4105DHP Bacteria
      COG0717 LUCA
      HOGENOMiHOG000228601
      InParanoidiP28248
      KOiK01494
      PhylomeDBiP28248

      Enzyme and pathway databases

      UniPathwayiUPA00610;UER00665
      BioCyciEcoCyc:DCTP-DEAM-MONOMER
      ECOL316407:JW2050-MONOMER
      MetaCyc:DCTP-DEAM-MONOMER
      BRENDAi3.5.4.13 2026

      Miscellaneous databases

      EvolutionaryTraceiP28248

      Protein Ontology

      More...
      PROi
      PR:P28248

      Family and domain databases

      CDDicd07557 trimeric_dUTPase, 1 hit
      Gene3Di2.70.40.10, 1 hit
      HAMAPiMF_00146 dCTP_deaminase, 1 hit
      InterProiView protein in InterPro
      IPR011962 dCTP_deaminase
      IPR029054 dUTPase-like
      IPR036157 dUTPase-like_sf
      IPR033704 dUTPase_trimeric
      PfamiView protein in Pfam
      PF00692 dUTPase, 1 hit
      SUPFAMiSSF51283 SSF51283, 1 hit
      TIGRFAMsiTIGR02274 dCTP_deam, 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 nameiDCD_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: P28248
      <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: December 1, 1992
      Last sequence update: December 1, 1992
      Last modified: September 18, 2019
      This is version 151 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, Direct protein sequencing, 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. Escherichia coli
        Escherichia coli (strain K12): entries and cross-references to EcoGene
      4. PATHWAY comments
        Index of metabolic and biosynthesis pathways
      UniProt is an ELIXIR core data resource
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