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CDD_MYCGE
ID   CDD_MYCGE               Reviewed;         130 AA.
AC   P47298;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Cytidine deaminase;
DE            Short=CDA;
DE            EC=3.5.4.5;
DE   AltName: Full=Cytidine aminohydrolase;
GN   Name=cdd; OrderedLocusNames=MG052;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-130.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
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       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; L43967; AAC71268.1; -; Genomic_DNA.
DR   EMBL; U02108; AAD12378.1; -; Genomic_DNA.
DR   PIR; G64205; G64205.
DR   RefSeq; WP_010869308.1; NZ_AAGX01000003.1.
DR   AlphaFoldDB; P47298; -.
DR   SMR; P47298; -.
DR   STRING; 243273.MG_052; -.
DR   EnsemblBacteria; AAC71268; AAC71268; MG_052.
DR   KEGG; mge:MG_052; -.
DR   eggNOG; COG0295; Bacteria.
DR   HOGENOM; CLU_097262_1_2_14; -.
DR   OMA; LTHFTCV; -.
DR   OrthoDB; 1895660at2; -.
DR   BioCyc; MGEN243273:G1GJ2-53-MON; -.
DR   Proteomes; UP000000807; Chromosome.
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:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0009972; P:cytidine deamination; IBA:GO_Central.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR006262; Cyt_deam_tetra.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR01354; cyt_deam_tetra; 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; Reference proteome; Zinc.
FT   CHAIN           1..130
FT                   /note="Cytidine deaminase"
FT                   /id="PRO_0000171679"
FT   DOMAIN          3..130
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        56
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         43..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   130 AA;  14974 MW;  1DF02B1718F9495F CRC64;
     MKVNLEWIIK QLQMIVKRAY TPFSNFKVAC MIIANNQTFF GVNIENSSFP VTLCAERSAI
     ASMVTSGHRK IDYVFVYFNT KNKSNSPCGM CRQNLLEFSH QKTKLFCIDN DSSYKQFSID
     ELLMNGFKKS
 
 
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