MUTT2_MYCTU
ID MUTT2_MYCTU Reviewed; 141 AA.
AC P9WIY1; 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 38.
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=Rv1160;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16585780; DOI=10.1128/jb.188.8.3159-3161.2006;
RA Dos Vultos T., Blazquez J., Rauzier J., Matic I., Gicquel B.;
RT "Identification of Nudix hydrolase family members with an antimutator role
RT in Mycobacterium tuberculosis and Mycobacterium smegmatis.";
RL J. Bacteriol. 188:3159-3161(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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). In vitro has 8-oxo-dGTPase
CC activity. {ECO:0000250, ECO:0000269|PubMed:16585780}.
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 -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16585780}.
CC -!- MISCELLANEOUS: There are 4 mutT paralogs in M.tuberculosis; the exact
CC function of each is unknown.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43916.1; -; Genomic_DNA.
DR PIR; A70556; A70556.
DR RefSeq; NP_215676.1; NC_000962.3.
DR RefSeq; WP_003406084.1; NZ_NVQJ01000025.1.
DR AlphaFoldDB; P9WIY1; -.
DR SMR; P9WIY1; -.
DR STRING; 83332.Rv1160; -.
DR PaxDb; P9WIY1; -.
DR DNASU; 888485; -.
DR GeneID; 888485; -.
DR KEGG; mtu:Rv1160; -.
DR TubercuList; Rv1160; -.
DR eggNOG; COG1051; Bacteria.
DR OMA; HADQPGM; -.
DR PhylomeDB; P9WIY1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; IBA:GO_Central.
DR GO; GO:0044716; F:8-oxo-GDP phosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA replication; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Mutator protein; Reference proteome.
FT CHAIN 1..141
FT /note="Putative 8-oxo-dGTP diphosphatase 2"
FT /id="PRO_0000391776"
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
