ID CDD_KLEV3 Reviewed; 294 AA. AC B5XP65; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 02-SEP-2026, entry version 82. 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=KPK_1584; OS Klebsiella variicola (strain 342) (Klebsiella pneumoniae). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Klebsiella; OC Klebsiella pneumoniae complex. OX NCBI_TaxID=507522; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=342; RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141; RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y., RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W., RA Methe B.A.; RT "Complete genome sequence of the N2-fixing broad host range endophyte RT Klebsiella pneumoniae 342 and virulence predictions verified in mice."; RL PLoS Genet. 4:E1000141-E1000141(2008). 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 + H2O + H(+) = uridine + NH4(+); 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 + H2O + H(+) = 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; CP000964; ACI09875.1; -; Genomic_DNA. DR AlphaFoldDB; B5XP65; -. DR SMR; B5XP65; -. DR KEGG; kpe:KPK_1584; -. DR HOGENOM; CLU_052424_0_0_6; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA. DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-ARBA. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0046135; P:pyrimidine nucleoside catabolic process; IEA:UniProtKB-ARBA. DR CDD; cd01283; cytidine_deaminase; 2. DR FunFam; 3.40.140.10:FF:000006; Cytidine deaminase; 1. DR FunFam; 3.40.140.10:FF:000007; Cytidine deaminase; 1. 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; IPR050202; Cyt/Deoxycyt_deaminase. 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 NCBIfam; NF006537; PRK09027.1; 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; Zinc. FT CHAIN 1..294 FT /note="Cytidine deaminase" FT /id="PRO_1000147105" 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; 31375 MW; 4DDB553318430AF6 CRC64; MHSRFQAALT TLAADLQAAI APMLADPHFP ALLEADQVAT LQQATGLDED ALAFALLPLA AACARADLSH FNVGAIARGV SGRWYFGGNM EFLGATMQQT VHAEQSAISH AWLRGETSLR AITVNYTPCG HCRQFMNELN SGLALRIHLP GREAHALEHY LPDAFGPKDL EIKTLLMDAQ DHGFPVSGDA LTQAAIQAAN RCHAPYSHSP SGVALELKDG TIFSGSYAEN AAFNPTLPPL QGALNLLSLN GYDYPAIQRA ILAEKADAAL IQWDATVATL KALGCQNIER VLLG //