CDD_SPOPS
ID CDD_SPOPS Reviewed; 136 AA.
AC Q9S3M0;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Cytidine deaminase;
DE Short=CDA;
DE EC=3.5.4.5;
DE AltName: Full=Cytidine aminohydrolase;
GN Name=cdd;
OS Sporosarcina psychrophila (Bacillus psychrophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11739901; DOI=10.1093/protein/14.10.807;
RA Cambi A., Vincenzetti S., De Sanctis G., Neuhard J., Natalini P., Vita A.;
RT "Cytidine deaminase from two extremophilic bacteria: cloning, expression
RT and comparison of their structural stability.";
RL Protein Eng. 14:807-813(2001).
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 -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AJ237978; CAB51906.1; -; Genomic_DNA.
DR RefSeq; WP_067208391.1; NZ_CP014616.1.
DR AlphaFoldDB; Q9S3M0; -.
DR SMR; Q9S3M0; -.
DR STRING; 1476.AZE41_09240; -.
DR OrthoDB; 1895660at2; -.
DR BRENDA; 3.5.4.5; 685.
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; 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; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..136
FT /note="Cytidine deaminase"
FT /id="PRO_0000171677"
FT DOMAIN 1..128
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 42..44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 86
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"
SQ SEQUENCE 136 AA; 14600 MW; 323DDC0450EC3E62 CRC64;
MDVEKLIAES KKAREQAYVP YSKFPVGAAL LAEDGTIYHG CNIENSAYSM TNCAERTAFF
KAVSDGVRSF KALAVVADTE GPVSPCGACR QVIAEFCNGS MPVYLTNLKG DIEETTVAKL
LPGAFSKEDL SYAAEQ
