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PEC Original Annotations
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Essentiality
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Class
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non-essential
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References (PMID)
|
Escherichia coli and Salmonella, Cellular and Molecular Biology Second Edition. ASM Press. 1996
Neidhart, F.C.
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Deletion
|
OCR30,31-3 (BK2-1 / AK1-1)
(D)
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Related gene (W3110 PEC)
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Gene Search
|
Search MG1655 PEC by gene name:
mutT
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Related strains
|
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Strains Search
|
Search strains by gene name:
mutT
Search strains by all related name:
mutT b0099 ECK0100 JW0097 nudA
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General information (Go to Linear View: )
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Gene Name
|
mutT
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Alternative name
|
b0099,ECK0100,JW0097,nudA
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Location, Length
|
111,044 - 111,433
(
+
)
;
2.39
min
;
390
(bp) ,
129
(aa)
|
|
Product
|
nucleoside triphosphate pyrophosphohydrolase, marked preference for dGTP
|
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Operon Name
|
secMA-mutT
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Note
|
7,8-dihydro-8-oxoguanine-triphosphatase, prefers dGTP, causes AT-GC transversions; GO_component: GO:0005737 - cytoplasm
|
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Function
|
enzyme; 2'-Deoxyribonucleotide metabolism
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Gene Ontology
|
GO:0000287
;
magnesium ion binding ( mutT )
GO:0004452
;
isopentenyl-diphosphate delta-isomerase activity ( mutT )
GO:0006260
;
DNA replication ( mutT )
GO:0006281
;
DNA repair ( mutT )
GO:0006974
;
response to DNA damage stimulus ( mutT )
GO:0008299
;
isoprenoid biosynthetic process ( mutT )
GO:0008413
;
8-oxo-7,8-dihydroguanine triphosphatase activity ( mutT )
GO:0016787
;
hydrolase activity ( mutT )
|
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PID
|
1786288
|
EC number
(KEGG Pathway)
|
3.6.1.-
|
|
Verified Protein Starts
(data
compiled from literature and appropriate citations are available from EcoGene)
|
|
EcoGene
|
mutT
(
EG10626
)
|
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Number of removed
|
0 aa cleaved
|
|
SWISS-PROT
(
Show details
[
2
more]
)
|
Entry name(Acc.no)
|
MUTT_ECOLI
(
P08337
)
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|
- Protein name
|
Mutator mutT protein
|
|
- Synonyms
|
7,8-dihydro-8-oxoguanine-triphosphatase, 8-oxo- dGTPase, EC 3.6.1.-, dGTP pyrophosphohydrolase
|
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- Gene name
|
Name=mutT; OrderedLocusNames=b0099;
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Homology Analysis
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BLAST
|
|
Bacteria
|
|
GTOP
|
mutT
(
homologous genes of other bacterias
)
|
|
PDB
(database updated :
2007.02.20
)
|
|
PSI-BLAST
|
Chain , Nmr Study Of Mutt Enzyme, A Nucleoside Triphosphate Pyrophosphohydrolase
|
|
SWISS-PROT
(database updated :
2007.02.20
)
|
|
BLAST
|
Mutator mutT protein
|
|
PSI-BLAST
|
Mutator mutT protein
|
|
nr
(database updated :
2007.02.20
)
|
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BLAST
|
nucleoside triphosphate pyrophosphohydrolase, marked preference for dGTP [Escherichia coli K12]
|
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Pfam 28.0
(database updated :
2015-05
)
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Pfam
|
|
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PROSITE
|
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PROSITE
|
PKC_PHOSPHO_SITE
CK2_PHOSPHO_SITE
MYRISTYL
MUTT
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MMBR References
|
J Bacteriol. 1994;176:7727-7729
Activity of the Escherichia coli mutT mutator allele in an anaerobic environment.
Fowler, R. G., J. A. Erickson, and R. J. Isbell.
|
J Bacteriol. 1968;96(4):975-80.
Selection of a mutant of Escherichia coli which has high mutation rates.
Helling RB.
(
4879569
)
|
Nature. 1992;355(6357):273-5.
MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis.
Maki H, Sekiguchi M.
(
1309939
)
|
J Biol Chem. 1988;263:8953-8957
Studies on the mutator gene, mutT, of Escherichia coli. Molecular cloning of the gene, purification of the gene product, and identification of a novel nucleoside triphosphatase.
Bhatnagar, S. K., and M. J. Bessman.
|
Mol Gen Genet. 1987;206(1):9-16.
Molecular cloning and nucleotide sequence of the mutT mutator of Escherichia coli that causes A:T to C:G transversion.
Akiyama M, Horiuchi T, Sekiguchi M.
(
3033442
)
|
J Bacteriol. 1967;94(1):38-47.
Mutator gene of Escherichia coli B.
Siegel EC, Bryson V.
(
5338974
)
|
Genetics 1974;77:169-184
Selection for high mutation rates in chemostats.
Cox, E. C., and T. Gibson.
|
| Sequences |
Amino acid
FASTA format
|
0001 MKKLQIAVGI IRNENNEIFI TRRAADAHMA NKLEFPGGKI EMGETPEQAV VRELQEEVGI TPQHFSLFEK
0071 LEYEFPDRHI TLWFWLVERW EGEPWGKEGQ PGEWMSLVGL NADDFPPANE PVIAKLKRL
|
Nucleotide
FASTA format
View sequence out neighbor 100bp
|
-100 CTGGTAAAAA ATACAAGCAG TGCCATGGCC
-070 GCCTGCAATA AAAGCTAACT GTTGAAGTAA AAGGCGCAGG ATTCTGCGCC TTTTTTATAG GTTTAAGACA
0001 atgaaaaagc tgcaaattgc ggtaggtatt attcgcaacg agaacaatga aatctttata acgcgtcgcg
0071 cagcagatgc gcacatggcg aataaactgg agtttcccgg cggtaaaatt gaaatgggtg aaacgccgga
0141 acaggcggtg gtgcgtgaac ttcaggaaga agtcgggatt accccccaac atttttcgct atttgaaaaa
0211 ctggaatatg aattcccgga caggcatata acactgtggt tttggctggt cgaacgctgg gaaggggagc
0281 cgtggggtaa agaagggcaa cccggtgagt ggatgtcgct ggtcggtctt aatgccgatg attttccgcc
0351 agccaatgaa ccggtaattg cgaagcttaa acgtctgtag GTCAGATAAG GCGTTTTCGC CGCATCCGAC
0421 ATTCGCACAC GATGCCTGAT GCGACGCTGG CGCGTCTTAT CAGGCCTAAA GGGATTTCTA ACTCATTGAT
|
