ID A0A1G2G602_9BACT Unreviewed; 336 AA.
AC A0A1G2G602;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN ORFNames=A2756_01770 {ECO:0000313|EMBL:OGZ45623.1};
OS Candidatus Ryanbacteria bacterium RIFCSPHIGHO2_01_FULL_48_27.
OC Bacteria; Candidatus Ryanbacteria.
OX NCBI_TaxID=1802115 {ECO:0000313|EMBL:OGZ45623.1, ECO:0000313|Proteomes:UP000177785};
RN [1] {ECO:0000313|EMBL:OGZ45623.1, ECO:0000313|Proteomes:UP000177785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00000878};
CC -!- SIMILARITY: Belongs to the dUTPase family.
CC {ECO:0000256|ARBA:ARBA00006581}.
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:OGZ45623.1}.
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DR EMBL; MHNL01000005; OGZ45623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2G602; -.
DR STRING; 1802115.A2756_01770; -.
DR Proteomes; UP000177785; Unassembled WGS sequence.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 2.70.40.10; -; 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; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR NCBIfam; TIGR00576; dut; 1.
DR PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF51283; dUTPase-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 Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 171..336
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 336 AA; 36147 MW; 6E4D0C2B1D347D1E CRC64;
MIIKIRKMFP DVKEPIRTSD GAVGYDVHAY RILDKFTKGV IGELPVTIEP HKSVLIGIGL
QLAVPPGIDC QLRPRSGLAT KHDIELGNSP GTLDPDFRGE AGVYLRNHGE APFTIKKGDR
IVQLVFTKVL LPEFVEVDTL PITVRNTGGF GATGLNGPGF GTDAYRAEVA RWDKYFMGIA
VSASSLSDCL RGVIKENGVY PVYEDGSYVG ATRKFGCVIT KDNIIIAQGY NTRTIECSEA
IGCVRENECI ASGIANDRGC LHAEEVAIQN HALSGGPSLR GTTIYVNAEP CVKCAKFLMG
CGIEAIVVPL GTFPTNGLKI LSDAGVEIRY IKTQSV
//
