ID I3TEQ3_THEC1 Unreviewed; 129 AA.
AC I3TEQ3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 OrderedLocusNames=TCELL_0817 {ECO:0000313|EMBL:AFK51241.1};
OS Thermogladius calderae (strain DSM 22663 / VKM B-2946 / 1633).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermogladius.
OX NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK51241.1, ECO:0000313|Proteomes:UP000005270};
RN [1] {ECO:0000313|EMBL:AFK51241.1, ECO:0000313|Proteomes:UP000005270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22663 / VKM B-2946 / 1633
RC {ECO:0000313|Proteomes:UP000005270};
RX PubMed=22843584; DOI=10.1128/JB.00894-12;
RA Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A.,
RA Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the hyperthermophilic cellulolytic
RT Crenarchaeon 'Thermogladius cellulolyticus' 1633.";
RL J. Bacteriol. 194:4446-4447(2012).
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; CP003531; AFK51241.1; -; Genomic_DNA.
DR RefSeq; WP_014737491.1; NC_017954.1.
DR AlphaFoldDB; I3TEQ3; -.
DR STRING; 1184251.TCELL_0817; -.
DR GeneID; 13013134; -.
DR KEGG; thg:TCELL_0817; -.
DR eggNOG; arCOG04173; Archaea.
DR HOGENOM; CLU_097262_4_1_2; -.
DR InParanoid; I3TEQ3; -.
DR OrthoDB; 39143at2157; -.
DR Proteomes; UP000005270; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005270};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..126
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 129 AA; 13901 MW; 08DE1B7220456ECF CRC64;
MRLLIEEAKR VLPHSYAPYS GVHVAAAVLT DKGNIYRGVN VENSSYGLTI CAERSAISAM
VTAGERRPVA IAIVTDMDEP IPPCGACRQV IAEFNSEAEV VMHSVKTGKT VVANLRDLFP
SPFKLRSTG
//
