MUTT3_MYCTU
ID MUTT3_MYCTU Reviewed; 217 AA.
AC P9WIX9; L0T5A7; P96259; Q7D9V1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Putative 8-oxo-dGTP diphosphatase 3;
DE Short=8-oxo-dGTPase;
DE EC=3.6.1.55;
DE AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase 3;
DE AltName: Full=Mutator protein MutT3;
DE AltName: Full=dGTP pyrophosphohydrolase 3;
GN Name=mutT3; OrderedLocusNames=Rv0413;
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 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). {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 -!- 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; CCP43144.1; -; Genomic_DNA.
DR PIR; C70629; C70629.
DR RefSeq; NP_214927.1; NC_000962.3.
DR RefSeq; WP_003402111.1; NC_000962.3.
DR AlphaFoldDB; P9WIX9; -.
DR SMR; P9WIX9; -.
DR STRING; 83332.Rv0413; -.
DR PaxDb; P9WIX9; -.
DR DNASU; 886405; -.
DR GeneID; 886405; -.
DR KEGG; mtu:Rv0413; -.
DR PATRIC; fig|83332.111.peg.453; -.
DR TubercuList; Rv0413; -.
DR eggNOG; COG0494; Bacteria.
DR OMA; HRAVWSH; -.
DR PhylomeDB; P9WIX9; -.
DR Proteomes; UP000001584; 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 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..217
FT /note="Putative 8-oxo-dGTP diphosphatase 3"
FT /id="PRO_0000391777"
FT DOMAIN 30..164
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 67..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 70..91
FT /note="Nudix box"
FT COMPBIAS 77..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 217 AA; 23499 MW; 3766660177EC04ED CRC64;
MPSCPPAYSE QVRGDGDGWV VSDSGVAYWG RYGAAGLLLR APRPDGTPAV LLQHRALWSH
QGGTWGLPGG ARDSHETPEQ TAVRESSEEA GLSAERLEVR ATVVTAEVCG VDDTHWTYTT
VVADAGELLD TVPNRESAEL RWVAENEVAD LPLHPGFAAS WQRLRTAPAT VPLARCDERR
QRLPRTIQIE AGVFLWCTPG DADQAPSPLG RRISSLL
