MUTT1_MYCTU
ID MUTT1_MYCTU Reviewed; 317 AA.
AC P9WIY3; 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:0000305};
DE Short=8-oxo-(d)GTPase {ECO:0000305};
DE EC=3.6.1.69 {ECO:0000269|PubMed:23463507};
DE AltName: Full=MtuMutT1 {ECO:0000303|PubMed:23463507};
DE AltName: Full=Mutator protein MutT1;
GN Name=mutT1 {ECO:0000303|PubMed:16585780}; OrderedLocusNames=Rv2985;
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=H37Rv;
RX PubMed=23463507; DOI=10.1074/jbc.m112.442566;
RA Patil A.G., Sang P.B., Govindan A., Varshney U.;
RT "Mycobacterium tuberculosis MutT1 (Rv2985) and ADPRase (Rv1700) proteins
RT constitute a two-stage mechanism of 8-oxo-dGTP and 8-oxo-GTP detoxification
RT and adenosine to cytidine mutation avoidance.";
RL J. Biol. Chem. 288:11252-11262(2013).
CC -!- FUNCTION: Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-
CC oxo-GTP to 8-oxo-GDP (PubMed:23463507, PubMed:16585780). Functions in
CC concert with Rv1700 to detoxify 8-oxo-dGTP to 8-oxo-dGMP and plays an
CC important role in supporting cellular growth under oxidative stress
CC (PubMed:23463507). {ECO:0000269|PubMed:16585780,
CC ECO:0000269|PubMed:23463507}.
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:0000269|PubMed:23463507};
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:0000269|PubMed:23463507};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0QUZ2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for 8-oxo-dGTP {ECO:0000269|PubMed:23463507};
CC Vmax=0.88 pmol/min/ng enzyme with 8-oxo-dGTP as substrate
CC {ECO:0000269|PubMed:23463507};
CC Note=kcat is 0.54 sec(-1) with 8-oxo-dGTP as substrate.
CC {ECO:0000269|PubMed:23463507};
CC -!- DISRUPTION PHENOTYPE: 15.5-fold spontaneous mutation frequency increase
CC by rifampicin resistance screening. {ECO:0000269|PubMed:16585780}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45790.1; -; Genomic_DNA.
DR PIR; F70673; F70673.
DR RefSeq; NP_217501.1; NC_000962.3.
DR RefSeq; WP_003899569.1; NZ_NVQJ01000041.1.
DR AlphaFoldDB; P9WIY3; -.
DR SMR; P9WIY3; -.
DR STRING; 83332.Rv2985; -.
DR PaxDb; P9WIY3; -.
DR DNASU; 888165; -.
DR GeneID; 45426974; -.
DR GeneID; 888165; -.
DR KEGG; mtu:Rv2985; -.
DR TubercuList; Rv2985; -.
DR eggNOG; COG0406; Bacteria.
DR eggNOG; COG0494; Bacteria.
DR OMA; RYDDWSW; -.
DR PhylomeDB; P9WIY3; -.
DR BioCyc; MetaCyc:G185E-7240-MON; -.
DR BRENDA; 3.6.1.69; 3445.
DR Proteomes; UP000001584; 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 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA replication; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..317
FT /note="8-oxo-(d)GTP phosphatase"
FT /id="PRO_0000391775"
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
