Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytosine deaminase

Gene

codA

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 hydrolytic deamination of cytosine to uracil. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis. Is also able to catalyze deamination of isoguanine, a mutagenic oxidation product of adenine in DNA, and of isocytosine. To a lesser extent, also catalyzes the conversion of 5-fluorocytosine (5FC) to 5-fluorouracil (5FU); this activity allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor.4 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 ‘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

Fe2+2 Publications, Mn2+1 Publication, Zn2+2 PublicationsNote: The purified enzyme contains a mixture of Fe2+ and Zn2+ bound in the active site, and a single equivalent of metal is required for full catalytic activity. After removal of the metal, the reconstitution of the enzyme with Fe2+ gives the highest activity, followed by Mn2+, and, to a much lesser extent, Co2+ and Zn2+.2 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

Fe2+-CDase is rapidly inactivated by H2O2, whereas Mn2+-CDase, Co2+-CDase, and Zn2+-CDase are not inactivated by H2O2. CDase is also inhibited by excess divalent cations (PubMed:8226944). Phosphonocytosine, a mimic of the tetrahedral reaction intermediate, inhibits the deamination of cytosine with a Ki of 52 nM (PubMed:21545144).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 185 sec(-1) for the deamination of cytosine using Fe2+ as cofactor, kcat is 92 sec(-1) using Mn2+ as cofactor, kcat is 52 sec(-1) using Co2+ as cofactor, and kcat is 32 sec(-1) using Zn2+ as cofactor (PubMed:8226944). kcat is 165 sec(-1) for the deamination of cytosine and 75.6 sec(-1) for the deamination of 5-fluorocytosine (PubMed:15381761). kcat is 132 sec(-1) for the deamination of cytosine, 5.1 sec(-1) for the deamination of isocytosine, 5.6 sec(-1) for the deamination of creatinine and 2.3 sec(-1) for the hydrolysis of 3-oxauracil (PubMed:21545144). kcat is 45 sec(-1) for the deamination of cytosine and 49 sec(-1) for the deamination of isoguanine at pH 7.7 (PubMed:21604715).4 Publications
  1. KM=0.22 mM for cytosine1 Publication
  2. KM=0.2 mM for cytosine1 Publication
  3. KM=3.3 mM for 5-fluorocytosine1 Publication
  4. KM=0.97 mM for cytosine1 Publication
  5. KM=0.46 mM for isocytosine1 Publication
  6. KM=25 mM for creatinine1 Publication
  7. KM=4.1 mM for 3-oxauracil1 Publication
  8. KM=72 µM for isoguanine1 Publication
  9. KM=302 µM for cytosine1 Publication

    pH dependencei

    Activity is lost under pH 5 but not affected up to pH 10.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi62Iron or zinc; catalytic6 Publications1
    Metal bindingi64Iron or zinc; catalytic6 Publications1
    <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 sitei157Substrate4 Publications1
    Metal bindingi215Iron or zinc; catalytic6 Publications1
    <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 sitei218Proton donor3 Publications1
    <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>Sitei247Activates the nucleophilic water2 Publications1
    Metal bindingi314Iron or zinc; catalytic6 Publications1
    Binding sitei320Substrate3 Publications1

    <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

    • cytosine catabolic process Source: EcoCyc

    <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 processCytosine metabolism
    LigandIron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

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

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.4.1 2026

    <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:
    Cytosine deaminase2 Publications (EC:3.5.4.14 Publications)
    Short name:
    CD1 Publication
    Short name:
    CDA1 Publication
    Short name:
    CDase1 Publication
    Alternative name(s):
    Cytosine aminohydrolase
    Isoguanine deaminase1 Publication (EC:3.5.4.-1 Publication)
    <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:codA
    Ordered Locus Names:b0337, JW0328
    <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
    EG11326 codA

    <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

    • cytosol Source: UniProtKB

    <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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Cytosine deaminase is being explored for use as a suicide gene for cancer gene therapy. The cytosine deaminase/5-fluorouracil combined therapy has been used successfully for a variety of animal tumor models and is currently under investigation for the treatment of human cancers.1 Publication1 Publication1 Publication

    <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

    Cells lacking this gene have less than 1% of the isoguanine deaminase activity of the wild-type strain.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>Mutagenesisi157Q → A or N: Less than 0.01% of wild-type enzymatic activity. 1 Publication1
    Mutagenesisi218E → A or Q: Less than 0.01% of wild-type enzymatic activity. 1 Publication1
    Mutagenesisi247H → A or N: Less than 0.01% of wild-type enzymatic activity. 1 Publication1
    Mutagenesisi247H → Q: 200-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi314D → A: 17-fold decrease in catalytic efficiency with cytosine as substrate and 2-fold increase in that with 5FC as substrate. Shows increased sensitivity to 5FC. 1 Publication1
    Mutagenesisi314D → A: Less than 0.01% of wild-type enzymatic activity. 1 Publication1
    Mutagenesisi314D → G or S: Still active towards cytosine. Shows increased sensitivity to 5FC. 1 Publication1
    Mutagenesisi314D → K, R or H: Loss of enzymatic activity. 1 Publication1
    Mutagenesisi314D → N: 35000-fold decrease in catalytic efficiency. 1 Publication1

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00000900022 – 427Cytosine deaminaseAdd BLAST426

    Proteomic databases

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

    More...
    PaxDbi
    P25524

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P25524

    <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

    Homohexamer.1 Publication

    <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

    WithEntry#Exp.IntActNotes
    itself3EBI-559181,EBI-559181

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4259813, 4 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-9306N

    Protein interaction database and analysis system

    More...
    IntActi
    P25524, 6 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316407.85674479

    <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

    1427
    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
    P25524

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

    More...
    SMRi
    P25524

    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
    P25524

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105DZC Bacteria
    COG0402 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000184778

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P25524

    KEGG Orthology (KO)

    More...
    KOi
    K01485

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P25524

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.30.40.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013108 Amidohydro_3
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07969 Amidohydro_3, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51338 SSF51338, 1 hit
    SSF51556 SSF51556, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P25524-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSNNALQTII NARLPGEEGL WQIHLQDGKI SAIDAQSGVM PITENSLDAE
    60 70 80 90 100
    QGLVIPPFVE PHIHLDTTQT AGQPNWNQSG TLFEGIERWA ERKALLTHDD
    110 120 130 140 150
    VKQRAWQTLK WQIANGIQHV RTHVDVSDAT LTALKAMLEV KQEVAPWIDL
    160 170 180 190 200
    QIVAFPQEGI LSYPNGEALL EEALRLGADV VGAIPHFEFT REYGVESLHK
    210 220 230 240 250
    TFALAQKYDR LIDVHCDEID DEQSRFVETV AALAHHEGMG ARVTASHTTA
    260 270 280 290 300
    MHSYNGAYTS RLFRLLKMSG INFVANPLVN IHLQGRFDTY PKRRGITRVK
    310 320 330 340 350
    EMLESGINVC FGHDDVFDPW YPLGTANMLQ VLHMGLHVCQ LMGYGQINDG
    360 370 380 390 400
    LNLITHHSAR TLNLQDYGIA AGNSANLIIL PAENGFDALR RQVPVRYSVR
    410 420
    GGKVIASTQP AQTTVYLEQP EAIDYKR
    Length:427
    Mass (Da):47,591
    Last modified:January 23, 2007 - v3
    <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:i9F91A2C46B3B1E42
    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 AAB18061 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti13R → W in strain: SO5076. 1

    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
    X63656 Genomic DNA Translation: CAA45196.1
    S56903 Genomic DNA Translation: AAB25761.2
    U73857 Genomic DNA Translation: AAB18061.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73440.1
    AP009048 Genomic DNA Translation: BAE76119.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S22662

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_414871.1, NC_000913.3
    WP_001301240.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73440; AAC73440; b0337
    BAE76119; BAE76119; BAE76119

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    944996

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0328
    eco:b0337

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1940

    <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
    X63656 Genomic DNA Translation: CAA45196.1
    S56903 Genomic DNA Translation: AAB25761.2
    U73857 Genomic DNA Translation: AAB18061.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73440.1
    AP009048 Genomic DNA Translation: BAE76119.1
    PIRiS22662
    RefSeqiNP_414871.1, NC_000913.3
    WP_001301240.1, 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
    1K6WX-ray1.75A2-427[»]
    1K70X-ray1.80A2-427[»]
    1R9XX-ray1.58A2-427[»]
    1R9YX-ray1.57A2-427[»]
    1R9ZX-ray1.32A2-427[»]
    1RA0X-ray1.12A2-427[»]
    1RA5X-ray1.40A2-427[»]
    1RAKX-ray1.32A2-427[»]
    3G77X-ray1.80A5-427[»]
    3O7UX-ray1.71A1-427[»]
    3R0DX-ray1.50A1-427[»]
    3RN6X-ray2.26A1-427[»]
    ProteinModelPortaliP25524
    SMRiP25524
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259813, 4 interactors
    DIPiDIP-9306N
    IntActiP25524, 6 interactors
    STRINGi316407.85674479

    Proteomic databases

    PaxDbiP25524
    PRIDEiP25524

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73440; AAC73440; b0337
    BAE76119; BAE76119; BAE76119
    GeneIDi944996
    KEGGiecj:JW0328
    eco:b0337
    PATRICifig|1411691.4.peg.1940

    Organism-specific databases

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

    More...
    EchoBASEi
    EB1302
    EcoGeneiEG11326 codA

    Phylogenomic databases

    eggNOGiENOG4105DZC Bacteria
    COG0402 LUCA
    HOGENOMiHOG000184778
    InParanoidiP25524
    KOiK01485
    PhylomeDBiP25524

    Enzyme and pathway databases

    BioCyciEcoCyc:CYTDEAM-MONOMER
    MetaCyc:CYTDEAM-MONOMER
    BRENDAi3.5.4.1 2026

    Miscellaneous databases

    EvolutionaryTraceiP25524

    Protein Ontology

    More...
    PROi
    PR:P25524

    Family and domain databases

    Gene3Di2.30.40.10, 1 hit
    InterProiView protein in InterPro
    IPR013108 Amidohydro_3
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase
    PfamiView protein in Pfam
    PF07969 Amidohydro_3, 1 hit
    SUPFAMiSSF51338 SSF51338, 1 hit
    SSF51556 SSF51556, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiCODA_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: P25524
    Secondary accession number(s): Q2MC87
    <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: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 147 of the entry and version 3 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again