ID Q8DZY9_STRA5 Unreviewed; 129 AA.
AC Q8DZY9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 95.
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 Name=cdd {ECO:0000313|EMBL:AAM99837.1};
GN OrderedLocusNames=SAG0953 {ECO:0000313|EMBL:AAM99837.1};
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435 {ECO:0000313|EMBL:AAM99837.1, ECO:0000313|Proteomes:UP000000821};
RN [1] {ECO:0000313|EMBL:AAM99837.1, ECO:0000313|Proteomes:UP000000821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821};
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin S., Kolonay J.F., Umayam L.A., Madupu R., Lewis M.R.,
RA Radune D., Fedorova N.B., Scanlan D., Khouri H., Mulligan S., Carty H.A.,
RA Cline R.T., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C.,
RA Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R.,
RA Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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}.
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DR EMBL; AE009948; AAM99837.1; -; Genomic_DNA.
DR RefSeq; NP_687965.1; NC_004116.1.
DR RefSeq; WP_000526762.1; NC_004116.1.
DR AlphaFoldDB; Q8DZY9; -.
DR STRING; 208435.SAG0953; -.
DR GeneID; 66885875; -.
DR KEGG; sag:SAG0953; -.
DR PATRIC; fig|208435.3.peg.959; -.
DR HOGENOM; CLU_097262_1_2_9; -.
DR OMA; LTHFTCV; -.
DR OrthoDB; 9795347at2; -.
DR Proteomes; UP000000821; Chromosome.
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; 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:SF2; 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 Reference proteome {ECO:0000313|Proteomes:UP000000821};
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 129 AA; 14014 MW; 1D0A553CB019F115 CRC64;
MGNIELKKLA VKASENAYVP YSKFPVGAAL RTAEGKIFTG CNVENISYGL ANCAERTAIF
KAVSEGYKDF SEIAIYGNTE EPISPCGACR QVMVEFFNKN AKVTLIAKNG KTVETTVGEL
LPYSFVDLK
//