MUTT1_MYCTO
ID MUTT1_MYCTO Reviewed; 317 AA.
AC P9WIY2; L0TB80; P95110; Q7D6B2;
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=8-oxo-(d)GTP phosphatase {ECO:0000250|UniProtKB:P9WIY3};
DE Short=8-oxo-(d)GTPase {ECO:0000250|UniProtKB:P9WIY3};
DE EC=3.6.1.69 {ECO:0000250|UniProtKB:P9WIY3};
GN Name=mutT1 {ECO:0000250|UniProtKB:P9WIY3}; OrderedLocusNames=MT3063;
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: Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-
CC oxo-GTP to 8-oxo-GDP. {ECO:0000250|UniProtKB:P9WIY3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGTP + H2O = 8-oxo-dGDP + H(+) + phosphate;
CC Xref=Rhea:RHEA:59980, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:63715, ChEBI:CHEBI:77896; EC=3.6.1.69;
CC Evidence={ECO:0000250|UniProtKB:P9WIY3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-GTP + H2O = 8-oxo-GDP + H(+) + phosphate;
CC Xref=Rhea:RHEA:60032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:143553, ChEBI:CHEBI:143554;
CC EC=3.6.1.69; Evidence={ECO:0000250|UniProtKB:P9WIY3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0QUZ2};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47392.1; -; Genomic_DNA.
DR PIR; F70673; F70673.
DR RefSeq; WP_003899569.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WIY2; -.
DR SMR; P9WIY2; -.
DR EnsemblBacteria; AAK47392; AAK47392; MT3063.
DR GeneID; 45426974; -.
DR KEGG; mtc:MT3063; -.
DR PATRIC; fig|83331.31.peg.3306; -.
DR HOGENOM; CLU_048989_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine 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 CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
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; PF00300; His_Phos_1; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
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;
KW Metal-binding.
FT CHAIN 1..317
FT /note="8-oxo-(d)GTP phosphatase"
FT /id="PRO_0000427925"
FT DOMAIN 15..148
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 54..75
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 43..46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 53..55
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0QUZ2"
SQ SEQUENCE 317 AA; 34780 MW; 995932F0F5113C3C CRC64;
MSIQNSSARR RSAGRIVYAA GAVLWRPGSA DSEGPVEIAV IHRPRYDDWS LPKGKVDPGE
TAPVGAVREI LEETGHRANL GRRLLTVTYP TDSPFRGVKK VHYWAARSTG GEFTPGSEVD
ELIWLPVPDA MNKLDYAQDR KVLCRFAKHP ADTQTVLVVR HGTAGSKAHF SGDDSKRPLD
KRGRAQAEAL VPQLLAFGAT DVYAADRVRC HQTMEPLAAE LNVTIHNEPT LTEESYANNP
KRGRHRVLQI VEQVGTPVIC TQGKVIPDLI TWWCERDGVH PDKSRNRKGS TWVLSLSAGR
LVTADHIGGA LAANVRA
