ID D6GV32_PARA5 Unreviewed; 385 AA.
AC D6GV32;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=8-oxo-dGTP diphosphatase {ECO:0000256|ARBA:ARBA00038905};
DE EC=3.6.1.55 {ECO:0000256|ARBA:ARBA00038905};
GN ORFNames=BJBARM5_0334 {ECO:0000313|EMBL:EFD92959.1};
OS Candidatus Parvarchaeum acidophilus ARMAN-5.
OC Archaea; Candidatus Parvarchaeota; Parvarchaeum.
OX NCBI_TaxID=662762 {ECO:0000313|EMBL:EFD92959.1, ECO:0000313|Proteomes:UP000009376};
RN [1] {ECO:0000313|EMBL:EFD92959.1, ECO:0000313|Proteomes:UP000009376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20421484; DOI=10.1073/pnas.0914470107;
RA Baker B.J., Comolli L.R., Dick G.J., Hauser L.J., Hyatt D., Dill B.D.,
RA Land M.L., Verberkmoes N.C., Hettich R.L., Banfield J.F.;
RT "Enigmatic, ultrasmall, uncultivated Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8806-8811(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; EC=3.6.1.55;
CC Evidence={ECO:0000256|ARBA:ARBA00035861};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005582}.
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DR EMBL; GG745550; EFD92959.1; -; Genomic_DNA.
DR AlphaFoldDB; D6GV32; -.
DR Proteomes; UP000009376; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR047127; MutT-like.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR47707; 8-OXO-DGTP DIPHOSPHATASE; 1.
DR PANTHER; PTHR47707:SF1; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFD92959.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Mutator protein {ECO:0000256|ARBA:ARBA00022457};
KW Reference proteome {ECO:0000313|Proteomes:UP000009376}.
FT DOMAIN 9..135
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 385 AA; 44836 MW; 33178CBAF7AA517D CRC64;
MKAEKIVTAE GNGVVGIILI DGKFLIDLRN MRNHMYLWEL PGGGIEKGET PISALKRELW
EEIGIKIKNV EWLGSKNQSV HWGHTEFEHY FLITEIEGTP FPKALRELKE VKWVYPEELK
DILNLGWRFT DGMFFLSRKS DKYKELYASL RARDFRPSLG FTYFAYSGTV KTWWKEEKLN
PKIVFKEEEN ELKKLLLKCS GPVLEIGPGY GRLTDLILRN FKTVDLLELN PDFRTILMKR
FGHRINFIDG VAEKFKTNKK YNTIVCAEVI EHIKDPYSFI GNIRSALSKD GVFILTLDNT
ESAWRKVRDS YRKVYNASTP EYYKKLRLDS VTNLLENSGF NVNVSKIGYR YPVYMPLGQR
NLPIPQVQNK KQPYMFLITC VPYGL
//
