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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

Keywordsi

Molecular functionHydrolase, Mutator protein
Biological processDNA damage, DNA repair, DNA replication
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10626-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.

Pathology & Biotechi

Chemistry databases

DrugBankiDB02023. 8-Oxo-2'-Deoxy-Guanosine-5'-Monophosphate.

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

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR003561. Mutator_MutT.
IPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
PfamiView protein in Pfam
PF00293. NUDIX. 1 hit.
PRINTSiPR01401. MUTATORMUTT.
PR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR00586. mutt. 1 hit.
PROSITEiView protein in PROSITE
PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.

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.

Chemistry databases

DrugBankiDB02023. 8-Oxo-2'-Deoxy-Guanosine-5'-Monophosphate.

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.
MetaCyc:EG10626-MONOMER.
BRENDAi3.6.1.55. 2026.

Miscellaneous databases

EvolutionaryTraceiP08337.
PROiPR:P08337.

Family and domain databases

InterProiView protein in InterPro
IPR003561. Mutator_MutT.
IPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
PfamiView protein in Pfam
PF00293. NUDIX. 1 hit.
PRINTSiPR01401. MUTATORMUTT.
PR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR00586. mutt. 1 hit.
PROSITEiView protein in PROSITE
PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMUTT_ECOLI
AccessioniPrimary (citable) accession number: P08337
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: May 10, 2017
This is version 159 of the entry and version 1 of the sequence. See 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.