ID CDD_MYCGE Reviewed; 130 AA. AC P47298; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 126. DE RecName: Full=Cytidine deaminase; DE Short=CDA; DE EC=3.5.4.5; DE AltName: Full=Cytidine aminohydrolase; GN Name=cdd; OrderedLocusNames=MG052; OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) OS (Mycoplasmoides genitalium). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-130. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and CC 2'-deoxycytidine for UMP synthesis. {ECO:0000250}. 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 -!- 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000305}. 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; L43967; AAC71268.1; -; Genomic_DNA. DR EMBL; U02108; AAD12378.1; -; Genomic_DNA. DR PIR; G64205; G64205. DR RefSeq; WP_010869308.1; NZ_AAGX01000003.1. DR AlphaFoldDB; P47298; -. DR SMR; P47298; -. DR STRING; 243273.MG_052; -. DR KEGG; mge:MG_052; -. DR eggNOG; COG0295; Bacteria. DR HOGENOM; CLU_097262_1_2_14; -. DR InParanoid; P47298; -. DR OrthoDB; 9795347at2; -. DR BioCyc; MGEN243273:G1GJ2-53-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0009972; P:cytidine deamination; IBA:GO_Central. DR CDD; cd01283; cytidine_deaminase; 1. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_dom. DR InterPro; IPR006262; Cyt_deam_tetra. DR InterPro; IPR016193; Cytidine_deaminase-like. DR NCBIfam; TIGR01354; cyt_deam_tetra; 1. DR PANTHER; PTHR11644; CYTIDINE DEAMINASE; 1. DR PANTHER; PTHR11644:SF2; CYTIDINE DEAMINASE; 1. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR SUPFAM; SSF53927; Cytidine deaminase-like; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 3: Inferred from homology; KW Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..130 FT /note="Cytidine deaminase" FT /id="PRO_0000171679" FT DOMAIN 3..130 FT /note="CMP/dCMP-type deaminase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT ACT_SITE 56 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 43..45 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 54 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" SQ SEQUENCE 130 AA; 14974 MW; 1DF02B1718F9495F CRC64; MKVNLEWIIK QLQMIVKRAY TPFSNFKVAC MIIANNQTFF GVNIENSSFP VTLCAERSAI ASMVTSGHRK IDYVFVYFNT KNKSNSPCGM CRQNLLEFSH QKTKLFCIDN DSSYKQFSID ELLMNGFKKS //