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Description:
Mutator mutT protein (7,8-dihydro-8-oxoguanine-triphosphatase) (8-oxo-dGTPase) (EC 3.6.1.-) (dGTP pyrophosphohydrolase).
Molecular weight: 14927
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
07-MAR-2006, entry version 66.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein MUTT_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X04831 | CAA28523.1 | - |
| EMBL | M20791 | AAA24620.1 | - |
| EMBL | X55034 | CAA38876.1 | - |
| EMBL | D10483 | BAB96667.1 | - |
| EMBL | U00096 | AAC73210.1 | - |
| EMBL | D26562 | BAB96669.1 | - |
| PIR | A27890 | MVECMT. | |
| PDB | 1MUT | NMR | @=1-129. |
| PDB | 1PPX | NMR | A=1-129. |
| PDB | 1PUN | NMR | A=1-129. |
| PDB | 1PUQ | NMR | A=1-129. |
| PDB | 1PUS | NMR | A=1-129. |
| PDB | 1TUM | NMR | @=1-129. |
| GenomeReviews | U00096_GR | b0099.1 | |
| EchoBASE | EB0621 | -.1 | |
| EcoGene | EG10626 | mutT. | |
| BioCyc | EcoCyc:EG10626-MONOMER | -.1 | |
| LinkHub | P08337 | -.1 | |
| InterPro | IPR003561 | MutT. | |
| InterPro | IPR000086 | NUDIX_hydrolase. | |
| Pfam | PF00293 | NUDIX | 1. |
| PRINTS | PR01401 | MUTATORMUTT. | |
| PRINTS | PR00502 | NUDIXFAMILY. | |
| TIGRFAMs | TIGR00586 | mutt | 1. |
| PROSITE | PS00893 | NUDIX | 1. |
Keywords:
3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA replication; Hydrolase; Magnesium; Mutator protein.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=87201091; 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 MEDLINE=92334977; PubMed=1630901;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N.,
RA Isono K., Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the
RT 0-2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; 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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
RC STRAIN=K12;
RX MEDLINE=88298644; PubMed=2841285;
RA Schmidt M., Rollo E., Grodberg J., Oliver D.;
RT "Nucleotide sequence of the secA gene and secA(Ts) mutations
RT preventing protein export in Escherichia coli.";
RL J. Bacteriol. 170:3404-3414(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-129.
RC STRAIN=K12 / W3110;
RX MEDLINE=94261430; PubMed=8202364;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the
RT 2.4-4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [6]
RP PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX MEDLINE=88243762; PubMed=3288626;
RA Bhatnagar S.K., Bessman M.J.;
RT "Studies on the mutator gene, mutT of Escherichia coli. Molecular
RT cloning of the gene, purification of the gene product, and
RT identification of a novel nucleoside triphosphatase.";
RL J. Biol. Chem. 263:8953-8957(1988).
RN [7]
RP CHARACTERIZATION.
RX MEDLINE=91225007; PubMed=1851162;
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 [8]
RP FUNCTION.
RX MEDLINE=92114971; PubMed=1309939; DOI=10.1038/355273a0;
RA Maki H., Sekiguchi M.;
RT "MutT protein specifically hydrolyses a potent mutagenic substrate for
RT DNA synthesis.";
RL Nature 355:273-275(1992).
RN [9]
RP STRUCTURE BY NMR.
RX MEDLINE=96072737; PubMed=7578113;
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 [10]
RP STRUCTURE BY NMR.
RX MEDLINE=97178805; 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).
Feature:
CHAIN 1 129 Mutator mutT protein.
/FTId=PRO_0000056943.
MOTIF 38 59 Nudix box.
STRAND 3 5
STRAND 9 10
STRAND 12 13
TURN 14 16
STRAND 17 22
STRAND 24 25
STRAND 28 30
STRAND 33 34
STRAND 40 42
STRAND 44 45
TURN 46 47
HELIX 48 55
TURN 56 58
STRAND 61 62
STRAND 64 65
STRAND 72 72
STRAND 76 77
STRAND 79 81
STRAND 85 89
STRAND 91 92
STRAND 98 99
STRAND 103 109
TURN 112 114
STRAND 115 115
TURN 117 118
HELIX 120 126
TURN 127 127
Comments:
-!- FUNCTION: Involved in the GO system responsible for removing an
oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine)
from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite
dA and dC residues of template DNA with almost equal efficiency
thus leading to A.T to G.C transversions. MutT specifically
degrades 8-oxo-dGTP to the monophosphate.
-!- CATALYTIC ACTIVITY: 8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate.
-!- COFACTOR: Magnesium.
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the Nudix hydrolase family.
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Sequence length: 129
MKKLQIAVGI IRNENNEIFI TRRAADAHMA NKLEFPGGKI EMGETPEQAV VRELQEEVGI
TPQHFSLFEK LEYEFPDRHI TLWFWLVERW EGEPWGKEGQ PGEWMSLVGL NADDFPPANE
PVIAKLKRL