GenomeNet

Database: UniProt
Entry: S9RWF0_9RHOB
LinkDB: S9RWF0_9RHOB
Original site: S9RWF0_9RHOB 
ID   S9RWF0_9RHOB            Unreviewed;       130 AA.
AC   S9RWF0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=8-oxo-dGTP diphosphatase {ECO:0000256|ARBA:ARBA00040794};
DE            EC=3.6.1.55 {ECO:0000256|ARBA:ARBA00038905};
DE   AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase {ECO:0000256|ARBA:ARBA00042798};
DE   AltName: Full=Mutator protein MutT {ECO:0000256|ARBA:ARBA00041979};
DE   AltName: Full=dGTP pyrophosphohydrolase {ECO:0000256|ARBA:ARBA00041592};
GN   ORFNames=Salmuc_04080 {ECO:0000313|EMBL:EPX82355.1};
OS   Salipiger mucosus DSM 16094.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX82355.1, ECO:0000313|Proteomes:UP000015347};
RN   [1] {ECO:0000313|Proteomes:UP000015347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX   PubMed=25197501; DOI=10.4056/sigs.4909790;
RA   Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT   strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT   clade.";
RL   Stand. Genomic Sci. 9:1331-1343(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-oxo-GTP + H2O = 8-oxo-GMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:67616, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:143553, ChEBI:CHEBI:145694;
CC         Evidence={ECO:0000256|ARBA:ARBA00036904};
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         ECO:0000256|PIRSR:PIRSR603561-2};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC       {ECO:0000256|ARBA:ARBA00005582}.
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:EPX82355.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; APVH01000023; EPX82355.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9RWF0; -.
DR   STRING; 1123237.Salmuc_04080; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_037162_19_2_5; -.
DR   Proteomes; UP000015347; Unassembled WGS sequence.
DR   GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IEA:RHEA.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR003561; Mutator_MutT.
DR   InterPro; IPR047127; MutT-like.
DR   InterPro; IPR029119; MutY_C.
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   NCBIfam; TIGR00586; mutt; 1.
DR   PANTHER; PTHR47707; 8-OXO-DGTP DIPHOSPHATASE; 1.
DR   PANTHER; PTHR47707:SF1; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 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:EPX82355.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR603561-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603561-2};
KW   Mutator protein {ECO:0000256|ARBA:ARBA00022457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015347}.
FT   DOMAIN          1..128
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   BINDING         21
FT                   /ligand="8-oxo-dGTP"
FT                   /ligand_id="ChEBI:CHEBI:77896"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-1"
FT   BINDING         32..35
FT                   /ligand="8-oxo-dGTP"
FT                   /ligand_id="ChEBI:CHEBI:77896"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-1"
FT   BINDING         35
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-2"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-2"
SQ   SEQUENCE   130 AA;  14625 MW;  5D3C819DD7C4EBA7 CRC64;
     MILVSAVALI DVDGRVLIAQ RPEGKSMEGL WEFPGGKVEA GETPEAALIR ELDEELGIDT
     WESCLAPLTF ASHAYEDFHL LMPLFACRKW QGQPQSREGQ ALKWVGVREL RDYPMPPADL
     PLIPILRDWL
//
DBGET integrated database retrieval system