ID MUTT_BUCAI Reviewed; 124 AA.
AC P57298;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=8-oxo-dGTP diphosphatase;
DE Short=8-oxo-dGTPase;
DE EC=3.6.1.55 {ECO:0000250|UniProtKB:P08337};
DE AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase;
DE AltName: Full=Mutator protein MutT;
DE AltName: Full=dGTP pyrophosphohydrolase;
GN Name=mutT; OrderedLocusNames=BU202;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: Specifically hydrolyzes both 8-oxo-deoxyguanosine
CC triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP)
CC to the related monophosphates, thereby cleaning up the nucleotide pools
CC and preventing misincorporation of 8-oxoGua into DNA and RNA. It
CC prevents replicational errors by removing an oxidatively damaged form
CC of guanine (8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP
CC can be inserted opposite dA and dC residues of template DNA with almost
CC equal efficiency thus leading to A.T to G.C transversions.
CC {ECO:0000250|UniProtKB:P08337}.
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:0000250|UniProtKB:P08337};
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:0000250|UniProtKB:P08337};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08337};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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; BA000003; BAB12919.1; -; Genomic_DNA.
DR RefSeq; NP_240033.1; NC_002528.1.
DR RefSeq; WP_010896000.1; NC_002528.1.
DR AlphaFoldDB; P57298; -.
DR SMR; P57298; -.
DR STRING; 563178.BUAP5A_199; -.
DR EnsemblBacteria; BAB12919; BAB12919; BAB12919.
DR KEGG; buc:BU202; -.
DR PATRIC; fig|107806.10.peg.213; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_037162_19_2_6; -.
DR Proteomes; UP000001806; Chromosome.
DR GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR047127; MutT-like.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
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.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Hydrolase; Magnesium;
KW Metal-binding; Mutator protein; Reference proteome.
FT CHAIN 1..124
FT /note="8-oxo-dGTP diphosphatase"
FT /id="PRO_0000056944"
FT DOMAIN 1..118
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 26..47
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08337"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08337"
SQ SEQUENCE 124 AA; 15061 MW; E1120D460C70801F CRC64;
MELLSKKKVY ITRGKYKKNI WEFPGGKVKK HENIVHALKR ELLEEVGIIV LKINFFQYIE
YIYPEKKIKL YFFLKKKWKG RPYSIEGYTY LWKRLCHLRA LDFPLANHSV INALKKNNIL
IKFR
//
