ID CDD_ECO57 Reviewed; 294 AA. AC Q8X648; Q7AC93; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 3. DT 27-MAR-2024, entry version 125. DE RecName: Full=Cytidine deaminase {ECO:0000255|HAMAP-Rule:MF_01558}; DE EC=3.5.4.5 {ECO:0000255|HAMAP-Rule:MF_01558}; DE AltName: Full=Cytidine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_01558}; DE Short=CDA {ECO:0000255|HAMAP-Rule:MF_01558}; GN Name=cdd {ECO:0000255|HAMAP-Rule:MF_01558}; GN OrderedLocusNames=Z3398, ECs3035; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and CC 2'-deoxycytidine for UMP synthesis. {ECO:0000255|HAMAP-Rule:MF_01558}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine + H(+) + H2O = NH4(+) + uridine; CC Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01558}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+); CC Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01558}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01558}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_01558}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01558}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000255|HAMAP-Rule:MF_01558}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE005174; AAG57281.2; -; Genomic_DNA. DR EMBL; BA000007; BAB36458.1; -; Genomic_DNA. DR PIR; C91008; C91008. DR PIR; E85852; E85852. DR RefSeq; NP_311062.1; NC_002695.1. DR RefSeq; WP_000553550.1; NZ_VOAI01000001.1. DR AlphaFoldDB; Q8X648; -. DR SMR; Q8X648; -. DR STRING; 155864.Z3398; -. DR GeneID; 916739; -. DR KEGG; ece:Z3398; -. DR KEGG; ecs:ECs_3035; -. DR PATRIC; fig|386585.9.peg.3160; -. DR eggNOG; COG0295; Bacteria. DR HOGENOM; CLU_052424_0_0_6; -. DR OMA; NYSPCGH; -. DR Proteomes; UP000000558; Chromosome. DR Proteomes; UP000002519; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA. DR GO; GO:0042802; F:identical protein binding; IEA:UniProt. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR CDD; cd01283; cytidine_deaminase; 2. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2. DR HAMAP; MF_01558; Cyt_deam; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_dom. DR InterPro; IPR013171; Cyd/dCyd_deaminase_Zn-bd. DR InterPro; IPR006263; Cyt_deam_dimer. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR020797; Cytidine_deaminase_bacteria. DR NCBIfam; TIGR01355; cyt_deam_dimer; 1. DR PANTHER; PTHR11644; CYTIDINE DEAMINASE; 1. DR PANTHER; PTHR11644:SF2; CYTIDINE DEAMINASE; 1. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF08211; dCMP_cyt_deam_2; 1. DR PIRSF; PIRSF006334; Cdd_plus_pseudo; 1. DR SUPFAM; SSF53927; Cytidine deaminase-like; 2. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2. PE 3: Inferred from homology; KW Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..294 FT /note="Cytidine deaminase" FT /id="PRO_0000171650" FT DOMAIN 48..168 FT /note="CMP/dCMP-type deaminase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT DOMAIN 186..294 FT /note="CMP/dCMP-type deaminase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT ACT_SITE 104 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" FT BINDING 89..91 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" FT BINDING 129 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" SQ SEQUENCE 294 AA; 31541 MW; 69B5D87DA4B147DC CRC64; MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED ALAFALLPLA AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT VHAEQSAISH AWLSGEKALA AITVNYTPCG HCRQFMNELN SGLDLRIHLP GREAHALRDY LADAFGPKDL EIKTLLMDEQ DHGYALTGDA LSQAAIAAAN RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL QGALILLNLK GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHNIDR VLLA //