ID A0A430BI59_9SPHN Unreviewed; 147 AA.
AC A0A430BI59;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 11.
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=BRX43_09550 {ECO:0000313|EMBL:RSU50415.1};
OS Sphingomonas sp. S-NIH.Pt15_0812.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1920129 {ECO:0000313|EMBL:RSU50415.1, ECO:0000313|Proteomes:UP000287772};
RN [1] {ECO:0000313|EMBL:RSU50415.1, ECO:0000313|Proteomes:UP000287772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-NIH.Pt15_0812 {ECO:0000313|EMBL:RSU50415.1,
RC ECO:0000313|Proteomes:UP000287772};
RA Johnson R.C., Deming C., Conlan S., Zellmer C., Michelin A., Lee-Lin S.-Q.,
RA Thomas P.J., Park M., Weingarten R.A., Less J., Dekker J.P., Frank K.M.,
RA Musser K.A., Mcquiston J.R., Henderson D.K., Lau A.F., Palmore T.N.,
RA Segre J.A.;
RT "Genomic and Epidemiologic Investigation to Identify Sphingomonas koreensis
RT Point Sources in an Indolent Hospital Outbreak.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RSU50415.1}.
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DR EMBL; QLJH01000011; RSU50415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430BI59; -.
DR OrthoDB; 9795347at2; -.
DR Proteomes; UP000287772; 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:RSU50415.1};
KW Metal-binding {ECO:0000256|RuleBase:RU364006};
KW Reference proteome {ECO:0000313|Proteomes:UP000287772};
KW Zinc {ECO:0000256|RuleBase:RU364006}.
FT DOMAIN 1..142
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 147 AA; 14903 MW; E76EB3F2A6B90EB4 CRC64;
MTDEQLIQAA RDAARHAHAP YSRFAVGAAL LMEGGDIVTG ANVENASYGL SLCAETVAIA
TASASGRLRE IVAVAVIGGA MDAEGRPTGA QPVSPCGRCR QVINEAAQLG GRDLPVLCGA
AEGEAIARYR LSELLPAAFG PGDLGIS
//
