ID A0A0M4LMB5_9MICC Unreviewed; 161 AA.
AC A0A0M4LMB5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Oxidized purine nucleoside triphosphate hydrolase {ECO:0000256|ARBA:ARBA00026218};
DE EC=3.6.1.56 {ECO:0000256|ARBA:ARBA00026103};
DE AltName: Full=2-hydroxy-dATP diphosphatase {ECO:0000256|ARBA:ARBA00031927};
DE AltName: Full=7,8-dihydro-8-oxoguanine triphosphatase {ECO:0000256|ARBA:ARBA00030682};
DE AltName: Full=8-oxo-dGTPase {ECO:0000256|ARBA:ARBA00030634};
DE AltName: Full=Methylated purine nucleoside triphosphate hydrolase {ECO:0000256|ARBA:ARBA00032071};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 1 {ECO:0000256|ARBA:ARBA00029673};
GN ORFNames=AL755_07915 {ECO:0000313|EMBL:ALE05418.1};
OS Arthrobacter sp. ERGS1:01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE05418.1, ECO:0000313|Proteomes:UP000060433};
RN [1] {ECO:0000313|EMBL:ALE05418.1, ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE05418.1,
RC ECO:0000313|Proteomes:UP000060433};
RX PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT bacterium with prospective cold active industrial enzymes, isolated from
RT East Rathong glacier in India.";
RL J. Biotechnol. 214:139-140(2015).
RN [2] {ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:67392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:71395, ChEBI:CHEBI:172878;
CC Evidence={ECO:0000256|ARBA:ARBA00024596};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67393;
CC Evidence={ECO:0000256|ARBA:ARBA00024596};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-dATP + H2O = 2-oxo-dAMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:31583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63212, ChEBI:CHEBI:77897; EC=3.6.1.56;
CC Evidence={ECO:0000256|ARBA:ARBA00024459};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31584;
CC Evidence={ECO:0000256|ARBA:ARBA00024459};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dATP + H2O = 8-oxo-dAMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:65396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:71361, ChEBI:CHEBI:172871;
CC Evidence={ECO:0000256|ARBA:ARBA00024448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65397;
CC Evidence={ECO:0000256|ARBA:ARBA00024448};
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;
CC Evidence={ECO:0000256|ARBA:ARBA00024486};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31576;
CC Evidence={ECO:0000256|ARBA:ARBA00024486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-methyl-ATP = diphosphate + H(+) + N(6)-methyl-AMP;
CC Xref=Rhea:RHEA:67608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:144842, ChEBI:CHEBI:172873;
CC Evidence={ECO:0000256|ARBA:ARBA00024619};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67609;
CC Evidence={ECO:0000256|ARBA:ARBA00024619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-methyl-dATP = diphosphate + H(+) + N(6)-methyl-
CC dAMP; Xref=Rhea:RHEA:67604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:169976, ChEBI:CHEBI:172872;
CC Evidence={ECO:0000256|ARBA:ARBA00024624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67605;
CC Evidence={ECO:0000256|ARBA:ARBA00024624};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O(6)-methyl-dGTP = diphosphate + H(+) + O(6)-methyl-
CC dGMP; Xref=Rhea:RHEA:67600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:169974, ChEBI:CHEBI:169975;
CC Evidence={ECO:0000256|ARBA:ARBA00024503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67601;
CC Evidence={ECO:0000256|ARBA:ARBA00024503};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CP012479; ALE05418.1; -; Genomic_DNA.
DR RefSeq; WP_054010539.1; NZ_CP012479.1.
DR AlphaFoldDB; A0A0M4LMB5; -.
DR STRING; 1704044.AL755_07915; -.
DR KEGG; are:AL755_07915; -.
DR PATRIC; fig|1704044.3.peg.809; -.
DR OrthoDB; 9804563at2; -.
DR Proteomes; UP000060433; Chromosome.
DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042262; P:DNA protection; IEA:InterPro.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR003563; 8ODP.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR43758; 7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE; 1.
DR PANTHER; PTHR43758:SF2; OXIDIZED PURINE NUCLEOSIDE TRIPHOSPHATE HYDROLASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR01403; 8OXTPHPHTASE.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ALE05418.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000060433}.
FT DOMAIN 2..139
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 161 AA; 17431 MW; 67441AB205841EE3 CRC64;
MTAAAVTLCF LLRTRAGGEE VLLGLKKTGF GAGKVVGVGG HVESGETTQE AICREVMEEC
GIAVAQADLI PAGTVDFVFP AKPAWDMATT VYLCRNFSGQ AQESDEILPH WYPVGKLPRA
QMWADAVHWL PAFLSGERAH WRIEMNPDNE TVAASTRTLI T
//
