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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)DescriptionActionsGraphical viewLength
Binding sitei23Substrate1
Binding sitei28Substrate1
Metal bindingi38Magnesium; via carbonyl oxygen1
Metal bindingi53Magnesium1
Metal bindingi56Magnesium1
Metal bindingi57Magnesium1
Binding sitei119Substrate1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10626. mutT.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000569431 – 1298-oxo-dGTP diphosphataseAdd BLAST129

Proteomic databases

PaxDbiP08337.
PRIDEiP08337.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

1129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 12Combined sources11
Beta strandi16 – 22Combined sources7
Turni24 – 26Combined sources3
Turni28 – 31Combined sources4
Beta strandi37 – 39Combined sources3
Beta strandi40 – 42Combined sources3
Helixi46 – 57Combined sources12
Beta strandi59 – 75Combined sources17
Beta strandi78 – 92Combined sources15
Beta strandi98 – 100Combined sources3
Beta strandi103 – 107Combined sources5
Helixi112 – 114Combined sources3
Helixi117 – 119Combined sources3
Helixi120 – 128Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08337.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 129Nudix hydrolasePROSITE-ProRule annotationAdd BLAST129

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni6 – 8Substrate binding3
Regioni34 – 38Substrate binding5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi38 – 59Nudix boxAdd BLAST22

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.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP08337.
PRIDEiP08337.

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.
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...

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: November 2, 2016
This is version 156 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.