UniProtKB - P25524 (CODA_ECOLI)
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>sp|P25524|CODA_ECOLI Cytosine deaminase OS=Escherichia coli (strain K12) OX=83333 GN=codA PE=1 SV=3 MSNNALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITENSLDAEQGLVIPPFVE PHIHLDTTQTAGQPNWNQSGTLFEGIERWAERKALLTHDDVKQRAWQTLKWQIANGIQHV RTHVDVSDATLTALKAMLEVKQEVAPWIDLQIVAFPQEGILSYPNGEALLEEALRLGADV VGAIPHFEFTREYGVESLHKTFALAQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMG ARVTASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQGRFDTYPKRRGITRVK EMLESGINVCFGHDDVFDPWYPLGTANMLQVLHMGLHVCQLMGYGQINDGLNLITHHSAR TLNLQDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKVIASTQPAQTTVYLEQP EAIDYKRHelp videoAdd a publicationFeedback
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>Select a section on the left to see content.
<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>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.10"Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy."
Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.
Protein Eng. Des. Sel. 17:625-633(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF MUTANTS GLY-314; ALA-314 AND SER-315 UNCOMPLEXED AND IN COMPLEX WITH (4S)-5-FLUORO-4-HYDROXY-3,4-DIHYDROPYRIMIDIN-2(1H)-ONE AND IRON, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-314, BIOTECHNOLOGY. - Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM. - Ref.13"Rescue of the orphan enzyme isoguanine deaminase."
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.
Biochemistry 50:5555-5557(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
<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
- cytosineEC:3.5.4.1
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Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.10"Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy."
Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.
Protein Eng. Des. Sel. 17:625-633(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF MUTANTS GLY-314; ALA-314 AND SER-315 UNCOMPLEXED AND IN COMPLEX WITH (4S)-5-FLUORO-4-HYDROXY-3,4-DIHYDROPYRIMIDIN-2(1H)-ONE AND IRON, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-314, BIOTECHNOLOGY. - Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM. - Ref.13"Rescue of the orphan enzyme isoguanine deaminase."
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.
Biochemistry 50:5555-5557(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
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Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.10"Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy."
Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.
Protein Eng. Des. Sel. 17:625-633(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF MUTANTS GLY-314; ALA-314 AND SER-315 UNCOMPLEXED AND IN COMPLEX WITH (4S)-5-FLUORO-4-HYDROXY-3,4-DIHYDROPYRIMIDIN-2(1H)-ONE AND IRON, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-314, BIOTECHNOLOGY. - Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM. - Ref.13"Rescue of the orphan enzyme isoguanine deaminase."
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.
Biochemistry 50:5555-5557(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
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cytosine- Search proteins in UniProtKB for this molecule.
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+uracil- Search proteins in UniProtKB for this molecule.
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- H+
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Manual assertion based on experiment ini
- Ref.13"Rescue of the orphan enzyme isoguanine deaminase."
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.
Biochemistry 50:5555-5557(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
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+isoguanine- Search proteins in UniProtKB for this molecule.
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+xanthine- Search proteins in UniProtKB for this molecule.
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<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+
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Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
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Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
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- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
<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
Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
<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
Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION. - Ref.10"Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy."
Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.
Protein Eng. Des. Sel. 17:625-633(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF MUTANTS GLY-314; ALA-314 AND SER-315 UNCOMPLEXED AND IN COMPLEX WITH (4S)-5-FLUORO-4-HYDROXY-3,4-DIHYDROPYRIMIDIN-2(1H)-ONE AND IRON, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-314, BIOTECHNOLOGY. - Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM. - Ref.13"Rescue of the orphan enzyme isoguanine deaminase."
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.
Biochemistry 50:5555-5557(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
- KM=0.22 mM for cytosine1 Publication
Manual assertion based on experiment ini
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
- KM=0.2 mM for cytosine1 Publication
Manual assertion based on experiment ini
- Ref.10"Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy."
Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.
Protein Eng. Des. Sel. 17:625-633(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF MUTANTS GLY-314; ALA-314 AND SER-315 UNCOMPLEXED AND IN COMPLEX WITH (4S)-5-FLUORO-4-HYDROXY-3,4-DIHYDROPYRIMIDIN-2(1H)-ONE AND IRON, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-314, BIOTECHNOLOGY.
- KM=3.3 mM for 5-fluorocytosine1 Publication
Manual assertion based on experiment ini
- Ref.10"Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy."
Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.
Protein Eng. Des. Sel. 17:625-633(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF MUTANTS GLY-314; ALA-314 AND SER-315 UNCOMPLEXED AND IN COMPLEX WITH (4S)-5-FLUORO-4-HYDROXY-3,4-DIHYDROPYRIMIDIN-2(1H)-ONE AND IRON, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-314, BIOTECHNOLOGY.
- KM=0.97 mM for cytosine1 Publication
Manual assertion based on experiment ini
- Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
- KM=0.46 mM for isocytosine1 Publication
Manual assertion based on experiment ini
- Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
- KM=25 mM for creatinine1 Publication
Manual assertion based on experiment ini
- Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
- KM=4.1 mM for 3-oxauracil1 Publication
Manual assertion based on experiment ini
- Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
- KM=72 µM for isoguanine1 Publication
Manual assertion based on experiment ini
- Ref.13"Rescue of the orphan enzyme isoguanine deaminase."
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.
Biochemistry 50:5555-5557(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
- KM=302 µM for cytosine1 Publication
Manual assertion based on experiment ini
- Ref.13"Rescue of the orphan enzyme isoguanine deaminase."
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.
Biochemistry 50:5555-5557(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
pH dependencei
Activity is lost under pH 5 but not affected up to pH 10.1 Publication
Manual assertion based on experiment ini
- Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bindingi | 62 | Iron or zinc; catalytic6 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 64 | Iron or zinc; catalytic6 Publications Manual assertion based on experiment ini
| 1 | |
| <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 sitei | 157 | Substrate4 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 215 | Iron or zinc; catalytic6 Publications Manual assertion based on experiment ini
| 1 | |
| <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 sitei | 218 | Proton donor3 Publications <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <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>Sitei | 247 | Activates the nucleophilic water2 Publications Manual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 314 | Iron or zinc; catalytic6 Publications Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 320 | Substrate3 Publications Manual assertion based on experiment ini
| 1 |
<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
- 5-fluorocytosine deaminase activity Source: UniProtKB-EC
- cytosine deaminase activity Source: EcoCyc
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
- ferrous iron binding Source: EcoCycInferred from direct assayi
- Ref.6"Cytosine deaminase. The roles of divalent metal ions in catalysis."
Porter D.J., Austin E.A.
J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.9"The structure of Escherichia coli cytosine deaminase."
Ireton G.C., McDermott G., Black M.E., Stoddard B.L.
J. Mol. Biol. 315:687-697(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH A MECHANISM-BASED INHIBITOR AND IRON, REACTION MECHANISM, ACTIVE SITE.
- isoguanine deaminase activity Source: EcoCycInferred from direct assayi
- Ref.13"Rescue of the orphan enzyme isoguanine deaminase."
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.
Biochemistry 50:5555-5557(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
- zinc ion binding Source: EcoCycInferred from direct assayi
- Ref.12"Three-dimensional structure and catalytic mechanism of cytosine deaminase."
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
GO - Biological processi
- cytosine catabolic process Source: EcoCyc
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "Mapping of the gene for cytosine deaminase on the Escherichia coli chromosome."
de Haan P.G., Felix H.S., Peters R.
Antonie Van Leeuwenhoek 38:257-263(1972) [PubMed] [Europe PMC] [Abstract]
<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 function | Hydrolase |
| Biological process | Cytosine metabolism |
| Ligand | Iron, Metal-binding, Zinc |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:CYTDEAM-MONOMER ECOL316407:JW0328-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%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<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: CD1 Publication Manual assertion based on opinion ini
Short name: CDA1 Publication Manual assertion based on opinion ini
Short name: CDase1 Publication Manual assertion based on opinion ini
Alternative name(s): Cytosine aminohydrolase Isoguanine deaminase1 Publication Manual assertion based on opinion ini
Manual assertion based on experiment ini
|
| <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>Organismi | Escherichia 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 identifieri | 83333 [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 lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <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 |
|
<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: UniProtKBInferred from high throughput direct assayi
- "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis."
Lasserre J.P., Beyne E., Pyndiah S., Lapaillerie D., Claverol S., Bonneu M.
Electrophoresis 27:3306-3321(2006) [PubMed] [Europe PMC] [Abstract]
<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 Publication
Manual assertion based on opinion ini
- Ref.8"Gene-directed enzyme prodrug therapy."
Zhang J., Kale V., Chen M.
AAPS J. 17:102-110(2015) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW, BIOTECHNOLOGY.
Manual assertion inferred by curator fromi
- Ref.10"Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy."
Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.
Protein Eng. Des. Sel. 17:625-633(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF MUTANTS GLY-314; ALA-314 AND SER-315 UNCOMPLEXED AND IN COMPLEX WITH (4S)-5-FLUORO-4-HYDROXY-3,4-DIHYDROPYRIMIDIN-2(1H)-ONE AND IRON, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-314, BIOTECHNOLOGY.
Manual assertion based on experiment ini
- Ref.11"Bacterial cytosine deaminase mutants created by molecular engineering show improved 5-fluorocytosine-mediated cell killing in vitro and in vivo."
Fuchita M., Ardiani A., Zhao L., Serve K., Stoddard B.L., Black M.E.
Cancer Res. 69:4791-4799(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 5-427 OF MUTANT ALA-153/CYS-317/GLY-318 IN COMPLEX WITH IRON, BIOTECHNOLOGY.
<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
Manual assertion based on experiment ini
- Ref.13"Rescue of the orphan enzyme isoguanine deaminase."
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C., Raushel F.M.
Biochemistry 50:5555-5557(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 157 | Q → A or N: Less than 0.01% of wild-type enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 218 | E → A or Q: Less than 0.01% of wild-type enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 247 | H → A or N: Less than 0.01% of wild-type enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 247 | H → Q: 200-fold decrease in catalytic efficiency. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 314 | D → 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 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 314 | D → A: Less than 0.01% of wild-type enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 314 | D → G or S: Still active towards cytosine. Shows increased sensitivity to 5FC. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 314 | D → K, R or H: Loss of enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 314 | D → N: 35000-fold decrease in catalytic efficiency. 1 Publication Manual assertion based on experiment ini
| 1 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB03939 (4S)-4-hydroxy-3,4-dihydro-2(1H)-pyrimidinone DB04135 5-Fluoro-4-(S)-Hydroxy-3,4-Dihydropyrimidine |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 methioninei | Removed1 Publication Manual assertion based on experiment ini
| |||
| <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_0000090002 | 2 – 427 | Cytosine deaminaseAdd BLAST | 426 |
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 PublicationManual assertion based on experiment ini
- Ref.7"Crystallization and preliminary X-ray analysis of bacterial cytosine deaminase."
Ireton G.C., Black M.E., Stoddard B.L.
Acta Crystallogr. D 57:1643-1645(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="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 |
|---|---|---|
| itself | 3 | EBI-559181,EBI-559181 |
GO - Molecular functioni
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.9"The structure of Escherichia coli cytosine deaminase."
Ireton G.C., McDermott G., Black M.E., Stoddard B.L.
J. Mol. Biol. 315:687-697(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH A MECHANISM-BASED INHIBITOR AND IRON, REACTION MECHANISM, ACTIVE SITE.
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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 8 – 13 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 19 – 26 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 29 – 38 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 46 – 48 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 53 – 56 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 58 – 63 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 65 – 69 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 73 – 75 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 82 – 93 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 98 – 114 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| Beta strandi | 117 – 125 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 132 – 144 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Turni | 145 – 147 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 149 – 155 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 160 – 163 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 166 – 175 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 179 – 181 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 185 – 187 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 188 – 190 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 191 – 208 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| Beta strandi | 211 – 216 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 226 – 237 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 240 – 242 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 243 – 247 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 249 – 253 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 256 – 269 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Beta strandi | 272 – 275 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 277 – 283 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 284 – 287 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 299 – 304 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 309 – 311 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 316 – 318 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 328 – 338 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 344 – 348 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 349 – 354 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 356 – 361 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 368 – 370 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 373 – 375 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 377 – 384 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 385 – 391 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 396 – 400 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 403 – 407 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 413 – 423 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 |
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 | ENOG4105DZC Bacteria COG0402 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_031758_0_1_6 |
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%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 basketAdded to basket
« Hide
Show »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
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 varianti | 13 | R → W in strain: SO5076. | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P25524 | Cytosine deaminase | 427 | UniRef100_P25524 | |||
| Cytosine deaminase | 427 | |||||
| Cytosine deaminase | 427 | |||||
| Cytosine deaminase | 427 | |||||
| Cytosine deaminase | 427 | |||||
| +12 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P25524 | Cytosine deaminase | 427 | UniRef90_P25524 | |||
| Cytosine deaminase | 427 | |||||
| Cytosine deaminase | 427 | |||||
| Cytosine deaminase | 427 | |||||
| Cytosine deaminase | 427 | |||||
| +797 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P25524 | Cytosine deaminase | 427 | UniRef50_P25524 | |||
| Cytosine deaminase | 427 | |||||
| Cytosine deaminase | 427 | |||||
| Cytosine deaminase | 427 | |||||
| Cytosine deaminase | 427 | |||||
| +6194 | ||||||
<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 |
| PIRi | S22662 |
| RefSeqi | NP_414871.1, NC_000913.3 WP_001301240.1, NZ_SSZK01000097.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1K6W | X-ray | 1.75 | A | 2-427 | [»] | |
| 1K70 | X-ray | 1.80 | A | 2-427 | [»] | |
| 1R9X | X-ray | 1.58 | A | 2-427 | [»] | |
| 1R9Y | X-ray | 1.57 | A | 2-427 | [»] | |
| 1R9Z | X-ray | 1.32 | A | 2-427 | [»] | |
| 1RA0 | X-ray | 1.12 | A | 2-427 | [»] | |
| 1RA5 | X-ray | 1.40 | A | 2-427 | [»] | |
| 1RAK | X-ray | 1.32 | A | 2-427 | [»] | |
| 3G77 | X-ray | 1.80 | A | 5-427 | [»] | |
| 3O7U | X-ray | 1.71 | A | 1-427 | [»] | |
| 3R0D | X-ray | 1.50 | A | 1-427 | [»] | |
| 3RN6 | X-ray | 2.26 | A | 1-427 | [»] | |
| SMRi | P25524 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 4259813, 4 interactors 849391, 1 interactor |
| DIPi | DIP-9306N |
| IntActi | P25524, 6 interactors |
| STRINGi | 511145.b0337 |
Chemistry databases
| DrugBanki | DB03939 (4S)-4-hydroxy-3,4-dihydro-2(1H)-pyrimidinone DB04135 5-Fluoro-4-(S)-Hydroxy-3,4-Dihydropyrimidine |
Proteomic databases
| jPOSTi | P25524 |
| PaxDbi | P25524 |
| PRIDEi | P25524 |
Genome annotation databases
| EnsemblBacteriai | AAC73440; AAC73440; b0337 BAE76119; BAE76119; BAE76119 |
| GeneIDi | 944996 |
| KEGGi | ecj:JW0328 eco:b0337 |
| PATRICi | fig|1411691.4.peg.1940 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1302 |
Phylogenomic databases
| eggNOGi | ENOG4105DZC Bacteria COG0402 LUCA |
| HOGENOMi | CLU_031758_0_1_6 |
| InParanoidi | P25524 |
| KOi | K01485 |
| PhylomeDBi | P25524 |
Enzyme and pathway databases
| BioCyci | EcoCyc:CYTDEAM-MONOMER ECOL316407:JW0328-MONOMER MetaCyc:CYTDEAM-MONOMER |
| BRENDAi | 3.5.4.1 2026 |
Miscellaneous databases
| EvolutionaryTracei | P25524 |
Protein Ontology More...PROi | PR:P25524 |
Family and domain databases
| Gene3Di | 2.30.40.10, 1 hit |
| InterProi | View protein in InterPro IPR013108 Amidohydro_3 IPR011059 Metal-dep_hydrolase_composite IPR032466 Metal_Hydrolase |
| Pfami | View protein in Pfam PF07969 Amidohydro_3, 1 hit |
| SUPFAMi | SSF51338 SSF51338, 1 hit SSF51556 SSF51556, 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 namei | CODA_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>Accessioni | P25524Primary (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 historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | June 17, 2020 | |
| This is version 159 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic 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 proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
