ID CDD_SHIFL Reviewed; 294 AA. AC P0ABF7; P13652; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 119. 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=SF2228, S2357; OS Shigella flexneri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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; AE005674; AAN43750.1; -; Genomic_DNA. DR EMBL; AE014073; AAP17567.1; -; Genomic_DNA. DR RefSeq; NP_708043.1; NC_004337.2. DR RefSeq; WP_000553555.1; NZ_WPGW01000017.1. DR AlphaFoldDB; P0ABF7; -. DR SMR; P0ABF7; -. DR STRING; 198214.SF2228; -. DR PaxDb; 198214-SF2228; -. DR GeneID; 1025385; -. DR GeneID; 75172271; -. DR KEGG; sfl:SF2228; -. DR KEGG; sfx:S2357; -. DR PATRIC; fig|198214.7.peg.2669; -. DR HOGENOM; CLU_052424_0_0_6; -. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; 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_0000171667" 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; 31540 MW; F0B5CD68AB145D7D CRC64; MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED ALAFALLPLA AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT VHAEQSAISH AWLSGEKALA AITVNYTPCG HCRQFMNELN SGLDLRIHLP GREAHALRDY LPDAFGPKDL EIKTLLMDEQ DHGYALTGDA LSQAAIAAAN RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL QGALILLNLK GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHSIDR VLLA //