ID H6RUB8_BLASD Unreviewed; 261 AA.
AC H6RUB8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=8-oxo-dGTP diphosphatase {ECO:0000256|ARBA:ARBA00038905};
DE EC=3.6.1.55 {ECO:0000256|ARBA:ARBA00038905};
GN OrderedLocusNames=BLASA_0933 {ECO:0000313|EMBL:CCG01883.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG01883.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG01883.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG01883.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; FO117623; CCG01883.1; -; Genomic_DNA.
DR AlphaFoldDB; H6RUB8; -.
DR STRING; 1146883.BLASA_0933; -.
DR KEGG; bsd:BLASA_0933; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_1119182_0_0_11; -.
DR OrthoDB; 9804442at2; -.
DR Proteomes; UP000007517; Chromosome.
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; cd03425; MutT_pyrophosphohydrolase; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR047127; MutT-like.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR47707; 8-OXO-DGTP DIPHOSPHATASE; 1.
DR PANTHER; PTHR47707:SF1; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCG01883.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000007517}.
FT DOMAIN 117..248
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 261 AA; 28088 MW; EA92736255EDFCB7 CRC64;
MFRLRFTTLV EAPLTVAFDV ARALGRPWPV PLEEVVSVRP ERDVYAVARG RGWITHSRRF
TATGAGTLVD EQVDWDTGLP GIVSGVVDRL VLRGRVVRAM QAHLDGYAAA AAHRALDVVR
VVGAALVDGD RVLVAQRSGG RYDGCWEFPG GKVEPGESDL AALVRECAEE LRVDVVPQAF
LGEVLLDGVV AGGAPGASTM RVWWGRIAHG RPVAHEHAQL RWVGAADLDA LDWIPADRPL
LPAVRALLGL GGAPRRGRTS R
//
