MUTT1_MYCS2
ID MUTT1_MYCS2 Reviewed; 322 AA.
AC A0QUZ2; I7FJ40;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
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:28375146};
DE AltName: Full=8-oxo-(d)GDP phosphatase {ECO:0000305};
DE EC=3.6.1.58 {ECO:0000269|PubMed:28375146};
DE AltName: Full=Diadenosine hexaphosphate hydrolase {ECO:0000305};
DE Short=Ap6A hydrolase {ECO:0000305};
DE EC=3.6.1.61 {ECO:0000269|PubMed:28705712};
DE AltName: Full=MsMutT1 {ECO:0000303|PubMed:28375146};
GN Name=mutT1 {ECO:0000303|PubMed:16585780};
GN OrderedLocusNames=MSMEG_2390 {ECO:0000312|EMBL:ABK74793.1},
GN MSMEI_2330 {ECO:0000312|EMBL:AFP38798.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
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 [5]
RP CRYSTALLIZATION.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=23027750; DOI=10.1107/s1744309112035804;
RA Arif S.M., Patil A.G., Varshney U., Vijayan M.;
RT "Crystallization and preliminary X-ray studies of MutT1 (MSMEG_2390) from
RT Mycobacterium smegmatis.";
RL Acta Crystallogr. F 68:1214-1216(2012).
RN [6] {ECO:0007744|PDB:5GG5, ECO:0007744|PDB:5GG6, ECO:0007744|PDB:5GG7, ECO:0007744|PDB:5GG8, ECO:0007744|PDB:5GG9, ECO:0007744|PDB:5GGA, ECO:0007744|PDB:5GGB, ECO:0007744|PDB:5GGC, ECO:0007744|PDB:5GGD}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE;
RP SUBSTRATE ANALOGS AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=28375146; DOI=10.1107/s2059798317002534;
RA Arif S.M., Patil A.G., Varshney U., Vijayan M.;
RT "Biochemical and structural studies of Mycobacterium smegmatis MutT1, a
RT sanitization enzyme with unusual modes of association.";
RL Acta Crystallogr. D 73:349-364(2017).
RN [7] {ECO:0007744|PDB:5XD1, ECO:0007744|PDB:5XD2, ECO:0007744|PDB:5XD3, ECO:0007744|PDB:5XD4, ECO:0007744|PDB:5XD5}
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEXES WITH DIADENOSINE
RP POLYPHOSPHATES; ATP; MAGNESIUM AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=28705712; DOI=10.1016/j.jsb.2017.07.002;
RA Arif S.M., Varshney U., Vijayan M.;
RT "Hydrolysis of diadenosine polyphosphates. Exploration of an additional
RT role of Mycobacterium smegmatis MutT1.";
RL J. Struct. Biol. 199:165-176(2017).
CC -!- FUNCTION: Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-
CC oxo-GTP to 8-oxo-GDP (PubMed:16585780, PubMed:28375146). At high enzyme
CC concentrations, can also catalyze the conversion of 8-oxo-dGDP to 8-
CC oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP (PubMed:28375146). In addition,
CC catalyzes the hydrolysis of the diadenosine polyphosphates diadenosine
CC hexaphosphate (Ap6A), diadenosine pentaphosphate (Ap5A) and diadenosine
CC tetraphosphate (Ap4A) (PubMed:28705712). {ECO:0000269|PubMed:16585780,
CC ECO:0000269|PubMed:28375146, ECO:0000269|PubMed:28705712}.
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:28375146};
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:28375146};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGDP + H2O = 8-oxo-dGMP + H(+) + phosphate;
CC Xref=Rhea:RHEA:32063, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:63224, ChEBI:CHEBI:63715; EC=3.6.1.58;
CC Evidence={ECO:0000269|PubMed:28375146};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-GDP + H2O = 8-oxo-GMP + H(+) + phosphate;
CC Xref=Rhea:RHEA:62356, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:143554, ChEBI:CHEBI:145694;
CC EC=3.6.1.58; Evidence={ECO:0000269|PubMed:28375146};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = 2 ATP + 2
CC H(+); Xref=Rhea:RHEA:32043, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:63740; EC=3.6.1.61;
CC Evidence={ECO:0000269|PubMed:28705712};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = ADP + ATP +
CC 2 H(+); Xref=Rhea:RHEA:30527, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:62041, ChEBI:CHEBI:456216;
CC EC=3.6.1.61; Evidence={ECO:0000269|PubMed:28705712};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = AMP + ATP +
CC 2 H(+); Xref=Rhea:RHEA:32039, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58141, ChEBI:CHEBI:456215;
CC EC=3.6.1.61; Evidence={ECO:0000269|PubMed:28705712};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28375146, ECO:0000269|PubMed:28705712};
CC Note=Can also use Mn(2+), with lower efficiency.
CC {ECO:0000269|PubMed:28705712};
CC -!- ACTIVITY REGULATION: Ap4A hydrolysis is inhibited by fluoride ions.
CC {ECO:0000269|PubMed:28705712}.
CC -!- SUBUNIT: Forms head-to-tail homodimers. {ECO:0000269|PubMed:28375146}.
CC -!- DOMAIN: Contains an N-terminal Nudix hydrolase domain, followed by a
CC linker region and a C-terminal histidine phosphatase domain. The C-
CC terminal domain is necessary for efficient catalysis by the Nudix
CC hydrolase domain. {ECO:0000269|PubMed:28375146}.
CC -!- DISRUPTION PHENOTYPE: 12-fold spontaneous mutation frequency increase
CC by rifampicin resistance screening. {ECO:0000269|PubMed:16585780}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP38798.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK74793.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38798.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011728311.1; NZ_SIJM01000012.1.
DR RefSeq; YP_886730.1; NC_008596.1.
DR PDB; 5GG5; X-ray; 1.64 A; A=1-322.
DR PDB; 5GG6; X-ray; 1.75 A; A/B=1-322.
DR PDB; 5GG7; X-ray; 1.70 A; A/B=1-322.
DR PDB; 5GG8; X-ray; 1.85 A; A=1-322.
DR PDB; 5GG9; X-ray; 1.60 A; A=1-322.
DR PDB; 5GGA; X-ray; 1.75 A; A=1-322.
DR PDB; 5GGB; X-ray; 1.10 A; A=1-322.
DR PDB; 5GGC; X-ray; 1.85 A; A/B=1-322.
DR PDB; 5GGD; X-ray; 1.70 A; A/B=1-322.
DR PDB; 5XD1; X-ray; 1.60 A; A=1-322.
DR PDB; 5XD2; X-ray; 1.75 A; A=1-322.
DR PDB; 5XD3; X-ray; 1.78 A; A=1-322.
DR PDB; 5XD4; X-ray; 1.47 A; A=1-322.
DR PDB; 5XD5; X-ray; 1.75 A; A/B=1-322.
DR PDB; 6M65; X-ray; 1.44 A; A=1-322.
DR PDB; 6M69; X-ray; 1.50 A; A=1-322.
DR PDB; 6M6Y; X-ray; 1.50 A; A=1-322.
DR PDB; 6M72; X-ray; 1.60 A; A=1-322.
DR PDBsum; 5GG5; -.
DR PDBsum; 5GG6; -.
DR PDBsum; 5GG7; -.
DR PDBsum; 5GG8; -.
DR PDBsum; 5GG9; -.
DR PDBsum; 5GGA; -.
DR PDBsum; 5GGB; -.
DR PDBsum; 5GGC; -.
DR PDBsum; 5GGD; -.
DR PDBsum; 5XD1; -.
DR PDBsum; 5XD2; -.
DR PDBsum; 5XD3; -.
DR PDBsum; 5XD4; -.
DR PDBsum; 5XD5; -.
DR PDBsum; 6M65; -.
DR PDBsum; 6M69; -.
DR PDBsum; 6M6Y; -.
DR PDBsum; 6M72; -.
DR AlphaFoldDB; A0QUZ2; -.
DR SMR; A0QUZ2; -.
DR STRING; 246196.MSMEI_2330; -.
DR EnsemblBacteria; ABK74793; ABK74793; MSMEG_2390.
DR EnsemblBacteria; AFP38798; AFP38798; MSMEI_2330.
DR GeneID; 66733804; -.
DR KEGG; msg:MSMEI_2330; -.
DR KEGG; msm:MSMEG_2390; -.
DR PATRIC; fig|246196.19.peg.2354; -.
DR eggNOG; COG0406; Bacteria.
DR eggNOG; COG0494; Bacteria.
DR OMA; RYDDWSW; -.
DR BRENDA; 3.6.1.69; 3512.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0044716; F:8-oxo-GDP phosphatase 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 3D-structure; DNA damage; DNA repair; DNA replication; Hydrolase;
KW Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..322
FT /note="8-oxo-(d)GTP phosphatase"
FT /id="PRO_0000449349"
FT DOMAIN 22..156
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 66..87
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 55..58
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28375146"
FT BINDING 65..67
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28375146,
FT ECO:0000269|PubMed:28705712"
FT STRAND 23..34
FT /evidence="ECO:0007829|PDB:5GGB"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5GG6"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:5GGB"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 88..103
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 106..120
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:5GGB"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:5GGB"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:5GGB"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:5GGB"
SQ SEQUENCE 322 AA; 35923 MW; EC7AC99FBF4D351E CRC64;
MMPVDDLQEI PLSKDTTEKS KHTVRAAGAV LWRDASEHGG TTGHPATVEV AVIHRPRYDD
WSLPKGKLDQ GETEPVAAAR EIHEETGHTA VLGRRLGRVT YPIPQGTKRV WYWAAKSTGG
DFSPNDEVDK LVWLPVDAAM DQLQYPDDRK VLRRFVKRPV DTKTVLVVRH GTAGRRSRYK
GDDRKRPLDK RGRAQAEALV AQLMAFGATT LYAADRVRCH QTIEPLAQEL DQLIHNEPLL
TEEAYAADHK AARKRLLEIA GRPGNPVICT QGKVIPGLIE WWCERAKVRP ETTGNRKGST
WVLSLSDGEL VGADYLSPPD EK
