ID CDD_VIBCH Reviewed; 295 AA. AC Q9KSM5; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 114. 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}; OrderedLocusNames=VC_1231; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=243277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A., RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). 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; AE003852; AAF94390.1; -; Genomic_DNA. DR PIR; G82226; G82226. DR RefSeq; NP_230876.1; NC_002505.1. DR RefSeq; WP_001245905.1; NZ_LT906614.1. DR PDB; 4EG2; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-295. DR PDBsum; 4EG2; -. DR AlphaFoldDB; Q9KSM5; -. DR SMR; Q9KSM5; -. DR STRING; 243277.VC_1231; -. DR DNASU; 2614668; -. DR EnsemblBacteria; AAF94390; AAF94390; VC_1231. DR GeneID; 66939137; -. DR KEGG; vch:VC_1231; -. DR PATRIC; fig|243277.26.peg.1173; -. DR eggNOG; COG0295; Bacteria. DR HOGENOM; CLU_052424_0_0_6; -. DR Proteomes; UP000000584; Chromosome 1. 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; 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 1: Evidence at protein level; KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..295 FT /note="Cytidine deaminase" FT /id="PRO_0000171669" FT DOMAIN 48..168 FT /note="CMP/dCMP-type deaminase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT DOMAIN 187..295 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" FT HELIX 2..11 FT /evidence="ECO:0007829|PDB:4EG2" FT TURN 14..16 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 17..24 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 35..45 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 49..61 FT /evidence="ECO:0007829|PDB:4EG2" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 103..113 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 119..126 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 130..136 FT /evidence="ECO:0007829|PDB:4EG2" FT TURN 140..144 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 157..160 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 191..200 FT /evidence="ECO:0007829|PDB:4EG2" FT TURN 206..208 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 212..218 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 223..227 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 240..250 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 258..265 FT /evidence="ECO:0007829|PDB:4EG2" FT HELIX 274..284 FT /evidence="ECO:0007829|PDB:4EG2" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:4EG2" SQ SEQUENCE 295 AA; 31955 MW; 7AA766021089D736 CRC64; MRNRIEQALQ QMPASFAPYL RELVLAKDFD ATFSAEQYQQ LLTLSGLEDA DLRVALLPIA AAYSYAPISE FYVGAIVRGI SGRLYLGANM EFTGAQLGQT VHAEQCAISH AWMKGEKGVA DITINFSPCG HCRQFMNELT TASSLKIQLP KRAAKTLQEY LPESFGPADL GIDSGLMSPV NHGKTSDDDE ELIQQALRAM NISHSPYTQN FSGVALKMRS GAIYLGAYAE NAAFNPSLPP LQVALAQAMM MGESFEDIEA AALVESATGK ISHLADTQAT LEVINPDIPL SYLSL //