GenomeNet

Database: UniProt
Entry: A0A3S0V3K9_9MICC
LinkDB: A0A3S0V3K9_9MICC
Original site: A0A3S0V3K9_9MICC 
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}.
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   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
//
DBGET integrated database retrieval system