ID   CDD_MYCTO               Reviewed;         133 AA.
AC   P9WPH2; L0TEZ3; O53367; Q7D5Q5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Cytidine deaminase;
DE            Short=CDD;
DE            EC=3.5.4.5;
DE   AltName: Full=Cytidine aminohydrolase;
DE            Short=CDA;
GN   Name=cdd; OrderedLocusNames=MT3416;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Recycles cytidine and 2-deoxycytidine for uridine and 2-
CC       deoxyuridine synthesis, respectively. Catalyzes the hydrolytic
CC       deamination of cytidine and 2-deoxycytidine to form, respectively,
CC       uridine and 2-deoxyuridine (By similarity). {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       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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; AE000516; AAK47758.1; -; Genomic_DNA.
DR   PIR; B70843; B70843.
DR   RefSeq; WP_003417264.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPH2; -.
DR   SMR; P9WPH2; -.
DR   EnsemblBacteria; AAK47758; AAK47758; MT3416.
DR   GeneID; 45427315; -.
DR   KEGG; mtc:MT3416; -.
DR   PATRIC; fig|83331.31.peg.3675; -.
DR   HOGENOM; CLU_097262_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..133
FT                   /note="Cytidine deaminase"
FT                   /id="PRO_0000426952"
FT   DOMAIN          4..126
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        58
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         45..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   133 AA;  14072 MW;  B21C0B188CB8080E CRC64;
     MPDVDWNMLR GNATQAAAGA YVPYSRFAVG AAALVDDGRV VTGCNVENVS YGLTLCAECA
     VVCALHSTGG GRLLALACVD GHGSVLMPCG RCRQVLLEHG GSELLIDHPV RPRRLGDLLP
     DAFGLDDLPR ERR