ID A0A3B5AWW0_9TELE Unreviewed; 133 AA.
AC A0A3B5AWW0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cytidine deaminase {ECO:0000256|ARBA:ARBA00012783, ECO:0000256|RuleBase:RU364006};
DE EC=3.5.4.5 {ECO:0000256|ARBA:ARBA00012783, ECO:0000256|RuleBase:RU364006};
DE AltName: Full=Cytidine aminohydrolase {ECO:0000256|ARBA:ARBA00032005, ECO:0000256|RuleBase:RU364006};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000018007.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000018007.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC 2'-deoxycytidine for UMP synthesis. {ECO:0000256|ARBA:ARBA00003949,
CC ECO:0000256|RuleBase:RU364006}.
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:0000256|RuleBase:RU364006};
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:0000256|ARBA:ARBA00000393,
CC ECO:0000256|RuleBase:RU364006};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU364006};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|RuleBase:RU364006}.
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 AlphaFoldDB; A0A3B5AWW0; -.
DR STRING; 144197.ENSSPAP00000018007; -.
DR Ensembl; ENSSPAT00000018284.1; ENSSPAP00000018007.1; ENSSPAG00000013592.1.
DR GeneTree; ENSGT00940000167107; -.
DR Proteomes; UP000261400; Unplaced.
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; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
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 NCBIfam; TIGR01354; cyt_deam_tetra; 1.
DR PANTHER; PTHR11644; CYTIDINE DEAMINASE; 1.
DR PANTHER; PTHR11644:SF26; CYTIDINE DEAMINASE; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364006};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364006};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364006}.
FT DOMAIN 1..128
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 133 AA; 14339 MW; 5E3F571FAAE1CFFB CRC64;
MASTELVLKC MQARDMAYCP YSHFPVGAAI LTADGAIITG CNVENASYGL TVCAERTAIQ
RAVAEGHRQF SAIAVTCDIK DRFVGPCGAC RQVLMEFGSE WIVYLTKPDG SYKETSLSEL
LPLAFSPAHL GKN
//
