ID   CDD_PHOPR               Reviewed;         295 AA.
AC   Q6LRI0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=PBPRA1689;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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}.
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DR   EMBL; CR378668; CAG20096.1; -; Genomic_DNA.
DR   RefSeq; WP_011218408.1; NC_006370.1.
DR   AlphaFoldDB; Q6LRI0; -.
DR   SMR; Q6LRI0; -.
DR   STRING; 298386.PBPRA1689; -.
DR   KEGG; ppr:PBPRA1689; -.
DR   eggNOG; COG0295; Bacteria.
DR   HOGENOM; CLU_052424_0_0_6; -.
DR   Proteomes; UP000000593; Chromosome 1.
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..295
FT                   /note="Cytidine deaminase"
FT                   /id="PRO_0000171657"
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"
SQ   SEQUENCE   295 AA;  31604 MW;  DF9C05B25D6B58AB CRC64;
     MHAKIMDALG SLPSDLASAV KPIFEDANFD ATLSPEQFTT LLSTTHMTDS ELRVALLPIA
     AAYSVAPISK FFVGAIVRGE SGRLYFGANM EFVGASLSQT IHAEQSAISH AWIKGETGIT
     DITINYSPCG HCRQFMNELT TAKTLIVQLP EREEQTLQQY LPESFGPADL NITDALLGKI
     DHGMTIKETD EFVAIACKAA NGSHAPYTKN YSGVALKATD GKVFTGKYAE NAAFNPSLPP
     LQVALVNMNM AGYALTEIAE AALVEKADST ISHLSDTQTT LEALNPDIPL TYVAA
//