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Entry version 165 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
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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%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi62Fe(2+); catalytic3 Publications1
Metal bindingi62Zn(2+); catalytic3 Publications1
Metal bindingi64Fe(2+); catalytic3 Publications1
Metal bindingi64Zn(2+); catalytic3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei157Substrate4 Publications1
Metal bindingi215Fe(2+); catalytic3 Publications1
Metal bindingi215Zn(2+); catalytic3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active 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 bindingi314Fe(2+); catalytic3 Publications1
Metal bindingi314Zn(2+); catalytic3 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

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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:codA
Ordered Locus Names:b0337, JW0328
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<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%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03939, (4S)-4-hydroxy-3,4-dihydro-2(1H)-pyrimidinone
DB04135, (4S)-5-Fluoro-4-hydroxy-3,4-dihydro-2(1H)-pyrimidinone

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000900022 – 427Cytosine deaminaseAdd BLAST426

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P25524

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%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P25524
With#Exp.IntAct
itself3EBI-559181,EBI-559181

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4259813, 4 interactors
849391, 1 interactor

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
511145.b0337

<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

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

More...
SMRi
P25524

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
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
COG0402, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_031758_0_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P25524

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is 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. Extended N-terminus.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_SSZK01000097.1

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_SSZK01000097.1

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[»]
SMRiP25524
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259813, 4 interactors
849391, 1 interactor
DIPiDIP-9306N
IntActiP25524, 6 interactors
STRINGi511145.b0337

Chemistry databases

DrugBankiDB03939, (4S)-4-hydroxy-3,4-dihydro-2(1H)-pyrimidinone
DB04135, (4S)-5-Fluoro-4-hydroxy-3,4-dihydro-2(1H)-pyrimidinone

Proteomic databases

jPOSTiP25524
PaxDbiP25524
PRIDEiP25524

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

Phylogenomic databases

eggNOGiCOG0402, Bacteria
HOGENOMiCLU_031758_0_1_6
InParanoidiP25524
PhylomeDBiP25524

Enzyme and pathway databases

BioCyciEcoCyc:CYTDEAM-MONOMER
BRENDAi3.5.4.1, 2026

Miscellaneous databases

EvolutionaryTraceiP25524

Protein Ontology

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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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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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 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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 165 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, 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
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