ID   CDD_SPOPS               Reviewed;         136 AA.
AC   Q9S3M0;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-SEP-2023, entry version 84.
DE   RecName: Full=Cytidine deaminase;
DE            Short=CDA;
DE            EC=3.5.4.5;
DE   AltName: Full=Cytidine aminohydrolase;
GN   Name=cdd;
OS   Sporosarcina psychrophila (Bacillus psychrophilus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11739901; DOI=10.1093/protein/14.10.807;
RA   Cambi A., Vincenzetti S., De Sanctis G., Neuhard J., Natalini P., Vita A.;
RT   "Cytidine deaminase from two extremophilic bacteria: cloning, expression
RT   and comparison of their structural stability.";
RL   Protein Eng. 14:807-813(2001).
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   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ237978; CAB51906.1; -; Genomic_DNA.
DR   RefSeq; WP_067208391.1; NZ_CP014616.1.
DR   AlphaFoldDB; Q9S3M0; -.
DR   SMR; Q9S3M0; -.
DR   STRING; 1476.AZE41_09240; -.
DR   OrthoDB; 9795347at2; -.
DR   BRENDA; 3.5.4.5; 685.
DR   GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd01283; cytidine_deaminase; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
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; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..136
FT                   /note="Cytidine deaminase"
FT                   /id="PRO_0000171677"
FT   DOMAIN          1..128
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        55
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         42..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   136 AA;  14600 MW;  323DDC0450EC3E62 CRC64;
     MDVEKLIAES KKAREQAYVP YSKFPVGAAL LAEDGTIYHG CNIENSAYSM TNCAERTAFF
     KAVSDGVRSF KALAVVADTE GPVSPCGACR QVIAEFCNGS MPVYLTNLKG DIEETTVAKL
     LPGAFSKEDL SYAAEQ
//