ID A0A1H5T7K2_9EURY Unreviewed; 163 AA.
AC A0A1H5T7K2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=cytidine deaminase {ECO:0000256|ARBA:ARBA00012783};
DE EC=3.5.4.5 {ECO:0000256|ARBA:ARBA00012783};
DE AltName: Full=Cytidine aminohydrolase {ECO:0000256|ARBA:ARBA00032005};
GN Name=cdd {ECO:0000313|EMBL:QCC47383.1};
GN ORFNames=DV707_06745 {ECO:0000313|EMBL:QCC47383.1}, SAMN04488133_0199
GN {ECO:0000313|EMBL:SEF58785.1};
OS Halobellus limi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=699433 {ECO:0000313|EMBL:SEF58785.1, ECO:0000313|Proteomes:UP000236740};
RN [1] {ECO:0000313|EMBL:SEF58785.1, ECO:0000313|Proteomes:UP000236740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:SEF58785.1,
RC ECO:0000313|Proteomes:UP000236740};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCC47383.1, ECO:0000313|Proteomes:UP000296733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:QCC47383.1,
RC ECO:0000313|Proteomes:UP000296733};
RX PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL Nat. Commun. 10:1688-1688(2019).
CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC 2'-deoxycytidine for UMP synthesis. {ECO:0000256|ARBA:ARBA00003949}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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DR EMBL; CP031311; QCC47383.1; -; Genomic_DNA.
DR EMBL; FNVN01000001; SEF58785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5T7K2; -.
DR KEGG; hlm:DV707_06745; -.
DR OrthoDB; 39143at2157; -.
DR Proteomes; UP000236740; Unassembled WGS sequence.
DR Proteomes; UP000296733; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:0000313|EMBL:QCC47383.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000236740};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 9..136
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT REGION 139..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 163 AA; 16979 MW; FE6ABF65110B094F CRC64;
MTDEDGPRPT TGGLVERARD ALGDAYVPYS EYRVGAALRT ADGTVYTGCN IENANYSNSL
HAEEVAIAAA VQDGHREFDA IAVSSGARDG VTPCGMCRQT LAEFAGGDLR VVCDEGDGEA
TTYTLGELLP NTISLETLSA AEAERDSELA EDAPDGDASG ADR
//
