MUTT_ECOLI
ID MUTT_ECOLI Reviewed; 129 AA.
AC P08337;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=8-oxo-dGTP diphosphatase;
DE Short=8-oxo-dGTPase;
DE EC=3.6.1.55 {ECO:0000269|PubMed:1309939, ECO:0000269|PubMed:15850400, ECO:0000269|PubMed:23481913, ECO:0000269|PubMed:9311918};
DE AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase;
DE AltName: Full=Mutator protein MutT;
DE AltName: Full=dGTP pyrophosphohydrolase;
GN Name=mutT {ECO:0000303|PubMed:3033442}; OrderedLocusNames=b0099, JW0097;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3033442; DOI=10.1007/bf00326530;
RA Akiyama M., Horiuchi T., Sekiguchi M.;
RT "Molecular cloning and nucleotide sequence of the mutT mutator of
RT Escherichia coli that causes A:T to C:G transversion.";
RL Mol. Gen. Genet. 206:9-16(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
RC STRAIN=K12;
RX PubMed=2841285; DOI=10.1128/jb.170.8.3404-3414.1988;
RA Schmidt M., Rollo E., Grodberg J., Oliver D.;
RT "Nucleotide sequence of the secA gene and secA(Ts) mutations preventing
RT protein export in Escherichia coli.";
RL J. Bacteriol. 170:3404-3414(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-129.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [7]
RP PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX PubMed=3288626; DOI=10.1016/s0021-9258(18)68400-5;
RA Bhatnagar S.K., Bessman M.J.;
RT "Studies on the mutator gene, mutT of Escherichia coli. Molecular cloning
RT of the gene, purification of the gene product, and identification of a
RT novel nucleoside triphosphatase.";
RL J. Biol. Chem. 263:8953-8957(1988).
RN [8]
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1851162; DOI=10.1016/s0021-9258(18)31550-3;
RA Bhatnagar S.K., Bullions L.C., Bessman M.J.;
RT "Characterization of the mutT nucleoside triphosphatase of Escherichia
RT coli.";
RL J. Biol. Chem. 266:9050-9054(1991).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1309939; DOI=10.1038/355273a0;
RA Maki H., Sekiguchi M.;
RT "MutT protein specifically hydrolyses a potent mutagenic substrate for DNA
RT synthesis.";
RL Nature 355:273-275(1992).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7739614; DOI=10.1016/0921-8777(94)00062-b;
RA Tajiri T., Maki H., Sekiguchi M.;
RT "Functional cooperation of MutT, MutM and MutY proteins in preventing
RT mutations caused by spontaneous oxidation of guanine nucleotide in
RT Escherichia coli.";
RL Mutat. Res. 336:257-267(1995).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9311918; DOI=10.1126/science.278.5335.128;
RA Taddei F., Hayakawa H., Bouton M., Cirinesi A., Matic I., Sekiguchi M.,
RA Radman M.;
RT "Counteraction by MutT protein of transcriptional errors caused by
RT oxidative damage.";
RL Science 278:128-130(1997).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15850400; DOI=10.1021/bi047550k;
RA Ito R., Hayakawa H., Sekiguchi M., Ishibashi T.;
RT "Multiple enzyme activities of Escherichia coli MutT protein for
RT sanitization of DNA and RNA precursor pools.";
RL Biochemistry 44:6670-6674(2005).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23481913; DOI=10.1016/j.ab.2013.02.023;
RA Xu A., Desai A.M., Brenner S.E., Kirsch J.F.;
RT "A continuous fluorescence assay for the characterization of Nudix
RT hydrolases.";
RL Anal. Biochem. 437:178-184(2013).
RN [14]
RP FUNCTION.
RX PubMed=25294823; DOI=10.1093/nar/gku912;
RA Gordon A.J., Satory D., Wang M., Halliday J.A., Golding I., Herman C.;
RT "Removal of 8-oxo-GTP by MutT hydrolase is not a major contributor to
RT transcriptional fidelity.";
RL Nucleic Acids Res. 42:12015-12026(2014).
RN [15] {ECO:0007744|PDB:1MUT}
RP STRUCTURE BY NMR.
RX PubMed=7578113; DOI=10.1021/bi00046a006;
RA Abeygunawardana C., Weber D.J., Gittis A.G., Frick D.N., Lin J.,
RA Miller A.F., Bessman M.J., Mildvan A.S.;
RT "Solution structure of the MutT enzyme, a nucleoside triphosphate
RT pyrophosphohydrolase.";
RL Biochemistry 34:14997-15005(1995).
RN [16] {ECO:0007744|PDB:1TUM}
RP STRUCTURE BY NMR IN COMPLEX WITH MAGNESIUM IONS AND A SUBSTRATE ANALOG, AND
RP COFACTOR.
RX PubMed=9063868; DOI=10.1021/bi962619c;
RA Lin J., Abeygunawardana C., Frick D.N., Bessman M.J., Mildvan A.S.;
RT "Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and
RT mechanism of its pyrophosphohydrolase action.";
RL Biochemistry 36:1199-1211(1997).
RN [17] {ECO:0007744|PDB:1PPX, ECO:0007744|PDB:1PUN, ECO:0007744|PDB:1PUQ, ECO:0007744|PDB:1PUS}
RP STRUCTURE BY NMR IN COMPLEXES WITH MAGNESIUM IONS AND 8-OXO-DGMP, AND
RP COFACTOR.
RX PubMed=12939141; DOI=10.1021/bi030105p;
RA Massiah M.A., Saraswat V., Azurmendi H.F., Mildvan A.S.;
RT "Solution structure and NH exchange studies of the MutT
RT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound
RT product.";
RL Biochemistry 42:10140-10154(2003).
RN [18] {ECO:0007744|PDB:3A6S, ECO:0007744|PDB:3A6T, ECO:0007744|PDB:3A6U, ECO:0007744|PDB:3A6V}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH 8-OXO-GMP AND
RP MANGANESE IONS, AND SUBUNIT.
RX PubMed=19864691; DOI=10.1074/jbc.m109.066373;
RA Nakamura T., Meshitsuka S., Kitagawa S., Abe N., Yamada J., Ishino T.,
RA Nakano H., Tsuzuki T., Doi T., Kobayashi Y., Fujii S., Sekiguchi M.,
RA Yamagata Y.;
RT "Structural and dynamic features of the MutT protein in the recognition of
RT nucleotides with the mutagenic 8-oxoguanine base.";
RL J. Biol. Chem. 285:444-452(2010).
CC -!- FUNCTION: Specifically hydrolyzes both 8-oxo-deoxyguanosine
CC triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP)
CC to the related monophosphates, thereby cleaning up the nucleotide pools
CC and preventing misincorporation of 8-oxoGua into DNA and RNA
CC (PubMed:1309939, PubMed:9311918, PubMed:15850400). It prevents
CC replicational errors by removing an oxidatively damaged form of guanine
CC (8-oxo-dGTP) from DNA and the nucleotide pool (PubMed:1309939). 8-oxo-
CC dGTP can be inserted opposite dA and dC residues of template DNA with
CC almost equal efficiency thus leading to A.T to G.C transversions
CC (PubMed:1309939). MutT may also ensure transcriptional fidelity,
CC removing 8-oxo-GTP from the ribonucleotide triphosphate pool
CC (PubMed:9311918). However, due to the lower efficiency of RNA
CC polymerase 8-oxo-GTP incorporation, MutT is probably not a major
CC contributor to transcriptional fidelity (PubMed:25294823). It also
CC hydrolyzes 8-oxo-dGDP and 8-oxo-GDP to their monophosphate form
CC (PubMed:15850400). In vitro, can also use dGTP, dGDP and other various
CC nucleoside di- and triphosphates, with much lower efficiency
CC (PubMed:1851162, PubMed:1309939, PubMed:15850400, PubMed:23481913).
CC Works cooperatively with MutM and MutY to prevent accumulation in the
CC DNA of oxidized guanine residues (PubMed:7739614).
CC {ECO:0000269|PubMed:1309939, ECO:0000269|PubMed:15850400,
CC ECO:0000269|PubMed:1851162, ECO:0000269|PubMed:23481913,
CC ECO:0000269|PubMed:25294823, ECO:0000269|PubMed:7739614,
CC ECO:0000269|PubMed:9311918}.
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 Evidence={ECO:0000269|PubMed:1309939, ECO:0000269|PubMed:15850400,
CC ECO:0000269|PubMed:23481913, ECO:0000269|PubMed:9311918};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-GTP + H2O = 8-oxo-GMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:67616, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:143553, ChEBI:CHEBI:145694;
CC Evidence={ECO:0000269|PubMed:15850400, ECO:0000269|PubMed:23481913,
CC ECO:0000269|PubMed:9311918};
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;
CC Evidence={ECO:0000269|PubMed:15850400};
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 Evidence={ECO:0000269|PubMed:15850400};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12939141, ECO:0000269|PubMed:1851162,
CC ECO:0000269|PubMed:19864691, ECO:0000269|PubMed:9063868};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.058 uM for 8-oxo-dGDP {ECO:0000269|PubMed:15850400};
CC KM=0.081 uM for 8-oxo-dGTP {ECO:0000269|PubMed:15850400};
CC KM=0.48 uM for 8-oxo-dGTP {ECO:0000269|PubMed:1309939};
CC KM=0.045 uM for 8-oxo-GDP {ECO:0000269|PubMed:15850400};
CC KM=0.26 uM for 8-oxo-GTP {ECO:0000269|PubMed:15850400};
CC KM=170 uM for dGDP {ECO:0000269|PubMed:15850400};
CC KM=1100 uM for dGTP {ECO:0000269|PubMed:1309939,
CC ECO:0000269|PubMed:15850400};
CC KM=1500 uM for dGTP {ECO:0000269|PubMed:1851162};
CC KM=2200 uM for dCTP {ECO:0000269|PubMed:1851162};
CC KM=1700 uM for dCTP {ECO:0000269|PubMed:1309939};
CC KM=1800 uM for dTTP {ECO:0000269|PubMed:1309939};
CC KM=350 uM for GDP {ECO:0000269|PubMed:15850400};
CC KM=1000 uM for GTP {ECO:0000269|PubMed:15850400};
CC KM=1200 uM for GTP {ECO:0000269|PubMed:1309939};
CC KM=0.53 uM for 8-oxo-dGTP (at pH 7.6 and 37 degrees Celsius as
CC measured by the Fiske-SubbaRow assay) {ECO:0000269|PubMed:23481913};
CC KM=0.28 uM for 8-oxo-dGTP (at pH 7.6 and 37 degrees Celsius as
CC measured by the Pi sensor assay) {ECO:0000269|PubMed:23481913};
CC KM=0.9 uM for 8-oxo-GTP (at pH 7.6 and 37 degrees Celsius))
CC {ECO:0000269|PubMed:23481913};
CC Vmax=3.7 pmol/min/ng enzyme toward 8-oxo-dGDP
CC {ECO:0000269|PubMed:15850400};
CC Vmax=20 pmol/min/ng enzyme toward 8-oxo-dGTP
CC {ECO:0000269|PubMed:15850400};
CC Vmax=4.8 pmol/min/ng enzyme toward 8-oxo-GDP
CC {ECO:0000269|PubMed:15850400};
CC Vmax=22 pmol/min/ng enzyme toward 8-oxo-GTP
CC {ECO:0000269|PubMed:15850400};
CC Vmax=5.9 pmol/min/ng enzyme toward dGDP
CC {ECO:0000269|PubMed:15850400};
CC Vmax=44 pmol/min/ng enzyme toward dGTP {ECO:0000269|PubMed:15850400};
CC Vmax=3.5 pmol/min/mg enzyme toward GDP {ECO:0000269|PubMed:15850400};
CC Vmax=24 pmol/min/mg enzyme toward GTP {ECO:0000269|PubMed:15850400};
CC Note=kcat is 6.9 sec(-1) with 8-oxo-dGTP as substrate measured by the
CC Fiske-SubbaRow assay. kcat is 5.5 sec(-1) with 8-oxo-dGTP as
CC substrate measured by the Pi sensor assay. kcat is 11.2 sec(-1) with
CC 8-oxo-GTP as substrate. {ECO:0000269|PubMed:23481913};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:1851162};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19864691}.
CC -!- INTERACTION:
CC P08337; P0AC47: frdB; NbExp=4; IntAct=EBI-1121389, EBI-906724;
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene increases the rates of A:T
CC to C:G transversion a thousandfold over the wild type level.
CC {ECO:0000269|PubMed:7739614}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; X04831; CAA28523.1; -; Genomic_DNA.
DR EMBL; M20791; AAA24620.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38876.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73210.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96667.1; -; Genomic_DNA.
DR PIR; A27890; MVECMT.
DR RefSeq; NP_414641.1; NC_000913.3.
DR RefSeq; WP_000736007.1; NZ_SSZK01000004.1.
DR PDB; 1MUT; NMR; -; A=1-129.
DR PDB; 1PPX; NMR; -; A=1-129.
DR PDB; 1PUN; NMR; -; A=1-129.
DR PDB; 1PUQ; NMR; -; A=1-129.
DR PDB; 1PUS; NMR; -; A=1-129.
DR PDB; 1TUM; NMR; -; A=1-129.
DR PDB; 3A6S; X-ray; 1.80 A; A/B=1-129.
DR PDB; 3A6T; X-ray; 1.96 A; A=1-129.
DR PDB; 3A6U; X-ray; 2.56 A; A=1-129.
DR PDB; 3A6V; X-ray; 2.00 A; A/B=1-129.
DR PDBsum; 1MUT; -.
DR PDBsum; 1PPX; -.
DR PDBsum; 1PUN; -.
DR PDBsum; 1PUQ; -.
DR PDBsum; 1PUS; -.
DR PDBsum; 1TUM; -.
DR PDBsum; 3A6S; -.
DR PDBsum; 3A6T; -.
DR PDBsum; 3A6U; -.
DR PDBsum; 3A6V; -.
DR AlphaFoldDB; P08337; -.
DR BMRB; P08337; -.
DR SMR; P08337; -.
DR BioGRID; 4261888; 366.
DR BioGRID; 849225; 4.
DR DIP; DIP-10288N; -.
DR IntAct; P08337; 5.
DR STRING; 511145.b0099; -.
DR DrugBank; DB02023; 8-oxo-dGMP.
DR jPOST; P08337; -.
DR PaxDb; P08337; -.
DR PRIDE; P08337; -.
DR EnsemblBacteria; AAC73210; AAC73210; b0099.
DR EnsemblBacteria; BAB96667; BAB96667; BAB96667.
DR GeneID; 944824; -.
DR KEGG; ecj:JW0097; -.
DR KEGG; eco:b0099; -.
DR PATRIC; fig|1411691.4.peg.2181; -.
DR EchoBASE; EB0621; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_037162_19_2_6; -.
DR InParanoid; P08337; -.
DR OMA; KLEYQFP; -.
DR PhylomeDB; P08337; -.
DR BioCyc; EcoCyc:EG10626-MON; -.
DR BioCyc; MetaCyc:EG10626-MON; -.
DR BRENDA; 3.6.1.55; 2026.
DR SABIO-RK; P08337; -.
DR EvolutionaryTrace; P08337; -.
DR PRO; PR:P08337; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IDA:UniProtKB.
DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IDA:UniProtKB.
DR GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; IDA:EcoCyc.
DR GO; GO:0044716; F:8-oxo-GDP phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0006203; P:dGTP catabolic process; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR003561; Mutator_MutT.
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; PR01401; MUTATORMUTT.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR TIGRFAMs; TIGR00586; mutt; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA replication; Hydrolase; Magnesium; Metal-binding; Mutator protein;
KW Reference proteome.
FT CHAIN 1..129
FT /note="8-oxo-dGTP diphosphatase"
FT /id="PRO_0000056943"
FT DOMAIN 1..129
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 38..59
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 23
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000305|PubMed:19864691"
FT BINDING 28
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000305|PubMed:19864691"
FT BINDING 34..37
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000305|PubMed:19864691"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19864691"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19864691"
FT BINDING 119
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000305|PubMed:12939141,
FT ECO:0000305|PubMed:19864691"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:3A6S"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3A6S"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1PUQ"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:3A6T"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3A6S"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1MUT"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:3A6S"
FT STRAND 59..75
FT /evidence="ECO:0007829|PDB:3A6S"
FT STRAND 78..92
FT /evidence="ECO:0007829|PDB:3A6S"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1PUN"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3A6S"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3A6S"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3A6S"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:3A6S"
SQ SEQUENCE 129 AA; 14927 MW; 626287828DCEA53E CRC64;
MKKLQIAVGI IRNENNEIFI TRRAADAHMA NKLEFPGGKI EMGETPEQAV VRELQEEVGI
TPQHFSLFEK LEYEFPDRHI TLWFWLVERW EGEPWGKEGQ PGEWMSLVGL NADDFPPANE
PVIAKLKRL
