ID   MUTT2_MYCTO             Reviewed;         141 AA.
AC   P9WIY0; L0T5W0; O06558; Q7D8R0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Putative 8-oxo-dGTP diphosphatase 2;
DE            Short=8-oxo-dGTPase 2;
DE            EC=3.6.1.55;
DE   AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase 2;
DE   AltName: Full=Mutator protein MutT2;
DE   AltName: Full=dGTP pyrophosphohydrolase 2;
GN   Name=mutT2; OrderedLocusNames=MT1197;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: May be involved in the GO system responsible for removing an
CC       oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-
CC       dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite
CC       dA and dC residues of template DNA with almost equal efficiency thus
CC       leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-
CC       dGTP to the monophosphate (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45454.1; -; Genomic_DNA.
DR   PIR; A70556; A70556.
DR   RefSeq; WP_003406084.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIY0; -.
DR   SMR; P9WIY0; -.
DR   EnsemblBacteria; AAK45454; AAK45454; MT1197.
DR   KEGG; mtc:MT1197; -.
DR   PATRIC; fig|83331.31.peg.1297; -.
DR   HOGENOM; CLU_037162_19_0_11; -.
DR   Proteomes; UP000001020; 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   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   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 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; Manganese;
KW   Metal-binding; Mutator protein.
FT   CHAIN           1..141
FT                   /note="Putative 8-oxo-dGTP diphosphatase 2"
FT                   /id="PRO_0000427926"
FT   DOMAIN          2..131
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           37..58
FT                   /note="Nudix box"
FT   BINDING         37
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   141 AA;  15160 MW;  6BA8276A1D38413E CRC64;
     MLNQIVVAGA IVRGCTVLVA QRVRPPELAG RWELPGGKVA AGETERAALA RELAEELGLE
     VADLAVGDRV GDDIALNGTT TLRAYRVHLL GGEPRARDHR ALCWVTAAEL HDVDWVPADR
     GWIADLARTL NGSAADVHRR C