CDD_MYCPN
ID CDD_MYCPN Reviewed; 133 AA.
AC P75051;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cytidine deaminase;
DE Short=CDA;
DE EC=3.5.4.5;
DE AltName: Full=Cytidine aminohydrolase;
GN Name=cdd; OrderedLocusNames=MPN_065; ORFNames=MP089;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB95737.1; -; Genomic_DNA.
DR PIR; S73415; S73415.
DR RefSeq; NP_109753.1; NC_000912.1.
DR RefSeq; WP_010874422.1; NC_000912.1.
DR AlphaFoldDB; P75051; -.
DR SMR; P75051; -.
DR IntAct; P75051; 1.
DR STRING; 272634.MPN_065; -.
DR EnsemblBacteria; AAB95737; AAB95737; MPN_065.
DR GeneID; 66609293; -.
DR KEGG; mpn:MPN_065; -.
DR PATRIC; fig|272634.6.peg.66; -.
DR HOGENOM; CLU_097262_2_2_14; -.
DR OMA; LTHFTCV; -.
DR BioCyc; MPNE272634:G1GJ3-101-MON; -.
DR Proteomes; UP000000808; 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:0008270; F:zinc ion binding; IEA:InterPro.
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..133
FT /note="Cytidine deaminase"
FT /id="PRO_0000171681"
FT DOMAIN 3..131
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 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 133 AA; 15185 MW; EC87E73810DEA9C7 CRC64;
MKVDLDWVHH KLQEVVNHAY TPFSKFKVAC MLVANNQAFY GVNIENASYP VTLCAERSAI
ANMVTSIGKA TIDYVFVYFD TKTPTNSPCG MCRQNIFEFA TDKTQLFCIE KDKSFKQFTI
PEILKGGFRS YEQ
