ID   CDD_SALPB               Reviewed;         294 AA.
AC   A9N6L3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
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=SPAB_00833;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX66257.1; -; Genomic_DNA.
DR   RefSeq; WP_000553526.1; NC_010102.1.
DR   AlphaFoldDB; A9N6L3; -.
DR   SMR; A9N6L3; -.
DR   KEGG; spq:SPAB_00833; -.
DR   PATRIC; fig|1016998.12.peg.780; -.
DR   HOGENOM; CLU_052424_0_0_6; -.
DR   BioCyc; SENT1016998:SPAB_RS03430-MONOMER; -.
DR   Proteomes; UP000008556; Chromosome.
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; Zinc.
FT   CHAIN           1..294
FT                   /note="Cytidine deaminase"
FT                   /id="PRO_1000087796"
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;  31619 MW;  B9685CBDC800A8C8 CRC64;
     MHPRFQTAFA QLADNLQSAL APILADHHFP AMLTAEQVST LKNTAGLDED ALAFALLPLA
     AACARTDLSH FNVGAIARGV SGNWYFGANM EFLGATMQQT VHAEQSAISH AWLRGEKGLA
     AVTVNYTPCG HCRQFMNELN SGLDLRIHLP GRAPHTLRDY LPDAFGPKDL EIKTLLMDEQ
     DHGFTLTGDT LTQAAITAAN KSHMPYSHSP SGVALECKDG RIFTGSYAEN AAFNPTLPPL
     QGALNLLSLN GYDYADIQRA ILAEKGDAAL IQWDATAATL KALGCHNIDR VLLG
//