ID A0A3S0V3K9_9MICC Unreviewed; 159 AA.
AC A0A3S0V3K9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Cytidine deaminase {ECO:0000256|ARBA:ARBA00018266, 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};
GN ORFNames=D8M21_07690 {ECO:0000313|EMBL:RUQ21259.1};
OS Kocuria sp. HSID16901.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=2419505 {ECO:0000313|EMBL:RUQ21259.1, ECO:0000313|Proteomes:UP000277032};
RN [1] {ECO:0000313|EMBL:RUQ21259.1, ECO:0000313|Proteomes:UP000277032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSID16901 {ECO:0000313|EMBL:RUQ21259.1,
RC ECO:0000313|Proteomes:UP000277032};
RX PubMed=30578265;
RA Stubbendieck R.M., May D.S., Chevrette M.G., Temkin M.I.,
RA Wendt-Pienkowski E., Cagnazzo J., Carlson C.M., Gern J.E., Currie C.R.;
RT "Competition among nasal bacteria suggests a role for siderophore-mediated
RT interactions in shaping the human nasal microbiota.";
RL Appl. Environ. Microbiol. 0:0-0(2018).
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|ARBA:ARBA00000631,
CC 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|ARBA:ARBA00006576, ECO:0000256|RuleBase:RU364006}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUQ21259.1}.
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DR EMBL; RBLM01000004; RUQ21259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0V3K9; -.
DR Proteomes; UP000277032; Unassembled WGS sequence.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
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; 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:SF2; CYTIDINE DEAMINASE; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364006, ECO:0000313|EMBL:RUQ21259.1};
KW Metal-binding {ECO:0000256|RuleBase:RU364006};
KW Reference proteome {ECO:0000313|Proteomes:UP000277032};
KW Zinc {ECO:0000256|RuleBase:RU364006}.
FT DOMAIN 11..133
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 159 AA; 17135 MW; C52F42344FEC15BD CRC64;
MTTTNHTNGE APWEPLMLAA REALEHSYSP YSRYRVGAAA RTSDGRLVTG ANIENASYGV
TLCAECSLVS DLFRTGGGSL SEFVCVNGDG EVIMPCGRCR QLLNEHRAPN LQIMTPLGPR
TMDEVLPQAF GAADVGGNAL QNLRDQSQES SVQTRGHHE
//