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Protein

8-oxo-dGTP diphosphatase

Gene

mutT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate.1 Publication

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Kineticsi

  1. KM=0.058 µM for 8-oxo-dGDP1 Publication
  2. KM=170 µM for dGDP1 Publication
  3. KM=0.081 µM for 8-oxo-dGTP1 Publication
  4. KM=1100 µM for GTP1 Publication
  5. KM=0.045 µM for 8-oxo-GDP1 Publication
  6. KM=0.26 µM for 8-oxo-GTP1 Publication
  1. Vmax=3.7 pmol/min/ng enzyme toward 8-oxo-dGDP1 Publication
  2. Vmax=5.9 pmol/min/ng enzyme toward dGDP1 Publication
  3. Vmax=20 pmol/min/ng enzyme toward 8-oxo-dGTP1 Publication
  4. Vmax=44 pmol/min/ng enzyme toward GTP1 Publication
  5. Vmax=4.8 pmol/min/ng enzyme toward 8-oxo-GDP1 Publication
  6. Vmax=22 pmol/min/ng enzyme toward 8-oxo-GTP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei23 – 231Substrate
Binding sitei28 – 281Substrate
Metal bindingi38 – 381Magnesium; via carbonyl oxygen
Metal bindingi53 – 531Magnesium
Metal bindingi56 – 561Magnesium
Metal bindingi57 – 571Magnesium
Binding sitei119 – 1191Substrate

GO - Molecular functioni

  • 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity Source: EcoCyc
  • 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity Source: UniProtKB
  • 8-oxo-dGDP phosphatase activity Source: EcoCyc
  • 8-oxo-GDP phosphatase activity Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • manganese ion binding Source: EcoCyc

GO - Biological processi

  • DNA repair Source: UniProtKB
  • DNA replication Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Mutator protein

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10626-MONOMER.
ECOL316407:JW0097-MONOMER.
MetaCyc:EG10626-MONOMER.
BRENDAi3.6.1.55. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
8-oxo-dGTP diphosphatase (EC:3.6.1.55)
Short name:
8-oxo-dGTPase
Alternative name(s):
7,8-dihydro-8-oxoguanine-triphosphatase
Mutator protein MutT
dGTP pyrophosphohydrolase
Gene namesi
Name:mutT
Ordered Locus Names:b0099, JW0097
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10626. mutT.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1291298-oxo-dGTP diphosphatasePRO_0000056943Add
BLAST

Proteomic databases

PaxDbiP08337.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
frdBP0AC474EBI-1121389,EBI-906724

Protein-protein interaction databases

BioGridi4261888. 366 interactions.
DIPiDIP-10288N.
IntActiP08337. 5 interactions.
MINTiMINT-1239561.
STRINGi511145.b0099.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1211Combined sources
Beta strandi16 – 227Combined sources
Turni24 – 263Combined sources
Turni28 – 314Combined sources
Beta strandi37 – 393Combined sources
Beta strandi40 – 423Combined sources
Helixi46 – 5712Combined sources
Beta strandi59 – 7517Combined sources
Beta strandi78 – 9215Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi103 – 1075Combined sources
Helixi112 – 1143Combined sources
Helixi117 – 1193Combined sources
Helixi120 – 1289Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MUTNMR-A1-129[»]
1PPXNMR-A1-129[»]
1PUNNMR-A1-129[»]
1PUQNMR-A1-129[»]
1PUSNMR-A1-129[»]
1TUMNMR-A1-129[»]
3A6SX-ray1.80A/B1-129[»]
3A6TX-ray1.96A1-129[»]
3A6UX-ray2.56A1-129[»]
3A6VX-ray2.00A/B1-129[»]
ProteinModelPortaliP08337.
SMRiP08337. Positions 3-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08337.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 129129Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 83Substrate binding
Regioni34 – 385Substrate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi38 – 5922Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105M6F. Bacteria.
COG0494. LUCA.
HOGENOMiHOG000261967.
InParanoidiP08337.
KOiK03574.
OMAiRLHWCKV.
OrthoDBiEOG6W19NW.
PhylomeDBiP08337.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR003561. Mutator_MutT.
IPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PANTHERiPTHR22769:SF36. PTHR22769:SF36. 1 hit.
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01401. MUTATORMUTT.
PR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR00586. mutt. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLQIAVGI IRNENNEIFI TRRAADAHMA NKLEFPGGKI EMGETPEQAV
60 70 80 90 100
VRELQEEVGI TPQHFSLFEK LEYEFPDRHI TLWFWLVERW EGEPWGKEGQ
110 120
PGEWMSLVGL NADDFPPANE PVIAKLKRL
Length:129
Mass (Da):14,927
Last modified:August 1, 1988 - v1
Checksum:i626287828DCEA53E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04831 Genomic DNA. Translation: CAA28523.1.
M20791 Genomic DNA. Translation: AAA24620.1.
X55034 Genomic DNA. Translation: CAA38876.1.
U00096 Genomic DNA. Translation: AAC73210.1.
AP009048 Genomic DNA. Translation: BAB96667.1.
PIRiA27890. MVECMT.
RefSeqiNP_414641.1. NC_000913.3.
WP_000736007.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73210; AAC73210; b0099.
BAB96667; BAB96667; BAB96667.
GeneIDi944824.
KEGGiecj:JW0097.
eco:b0099.
PATRICi32115303. VBIEscCol129921_0103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04831 Genomic DNA. Translation: CAA28523.1.
M20791 Genomic DNA. Translation: AAA24620.1.
X55034 Genomic DNA. Translation: CAA38876.1.
U00096 Genomic DNA. Translation: AAC73210.1.
AP009048 Genomic DNA. Translation: BAB96667.1.
PIRiA27890. MVECMT.
RefSeqiNP_414641.1. NC_000913.3.
WP_000736007.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MUTNMR-A1-129[»]
1PPXNMR-A1-129[»]
1PUNNMR-A1-129[»]
1PUQNMR-A1-129[»]
1PUSNMR-A1-129[»]
1TUMNMR-A1-129[»]
3A6SX-ray1.80A/B1-129[»]
3A6TX-ray1.96A1-129[»]
3A6UX-ray2.56A1-129[»]
3A6VX-ray2.00A/B1-129[»]
ProteinModelPortaliP08337.
SMRiP08337. Positions 3-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261888. 366 interactions.
DIPiDIP-10288N.
IntActiP08337. 5 interactions.
MINTiMINT-1239561.
STRINGi511145.b0099.

Proteomic databases

PaxDbiP08337.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73210; AAC73210; b0099.
BAB96667; BAB96667; BAB96667.
GeneIDi944824.
KEGGiecj:JW0097.
eco:b0099.
PATRICi32115303. VBIEscCol129921_0103.

Organism-specific databases

EchoBASEiEB0621.
EcoGeneiEG10626. mutT.

Phylogenomic databases

eggNOGiENOG4105M6F. Bacteria.
COG0494. LUCA.
HOGENOMiHOG000261967.
InParanoidiP08337.
KOiK03574.
OMAiRLHWCKV.
OrthoDBiEOG6W19NW.
PhylomeDBiP08337.

Enzyme and pathway databases

BioCyciEcoCyc:EG10626-MONOMER.
ECOL316407:JW0097-MONOMER.
MetaCyc:EG10626-MONOMER.
BRENDAi3.6.1.55. 2026.

Miscellaneous databases

EvolutionaryTraceiP08337.
PROiP08337.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR003561. Mutator_MutT.
IPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PANTHERiPTHR22769:SF36. PTHR22769:SF36. 1 hit.
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01401. MUTATORMUTT.
PR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR00586. mutt. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    Mol. Gen. Genet. 206:9-16(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli."
    Schmidt M., Rollo E., Grodberg J., Oliver D.
    J. Bacteriol. 170:3404-3414(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
    Strain: K12.
  6. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-129.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "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., Bessman M.J.
    J. Biol. Chem. 263:8953-8957(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
    Strain: K12.
  8. "Characterization of the mutT nucleoside triphosphatase of Escherichia coli."
    Bhatnagar S.K., Bullions L.C., Bessman M.J.
    J. Biol. Chem. 266:9050-9054(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis."
    Maki H., Sekiguchi M.
    Nature 355:273-275(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools."
    Ito R., Hayakawa H., Sekiguchi M., Ishibashi T.
    Biochemistry 44:6670-6674(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
  11. "Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase."
    Abeygunawardana C., Weber D.J., Gittis A.G., Frick D.N., Lin J., Miller A.F., Bessman M.J., Mildvan A.S.
    Biochemistry 34:14997-15005(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  12. "Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and mechanism of its pyrophosphohydrolase action."
    Lin J., Abeygunawardana C., Frick D.N., Bessman M.J., Mildvan A.S.
    Biochemistry 36:1199-1211(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH MAGNESIUM IONS AND AMPCPP.
  13. "Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base."
    Nakamura T., Meshitsuka S., Kitagawa S., Abe N., Yamada J., Ishino T., Nakano H., Tsuzuki T., Doi T., Kobayashi Y., Fujii S., Sekiguchi M., Yamagata Y.
    J. Biol. Chem. 285:444-452(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH 8-OXO-GMP AND MANGANESE IONS.

Entry informationi

Entry nameiMUTT_ECOLI
AccessioniPrimary (citable) accession number: P08337
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 13, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.