UniProtKB - P08337 (MUTT_ECOLI)
8-oxo-dGTP diphosphatase
mutT
Functioni
Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA (PubMed:1309939, PubMed:9311918, PubMed:15850400).
It prevents replicational errors by removing an oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool (PubMed:1309939).
8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (PubMed:1309939).
MutT may also ensure transcriptional fidelity, removing 8-oxo-GTP from the ribonucleotide triphosphate pool (PubMed:9311918).
However, due to the lower efficiency of RNA polymerase 8-oxo-GTP incorporation, MutT is probably not a major contributor to transcriptional fidelity (PubMed:25294823).
It also hydrolyzes 8-oxo-dGDP and 8-oxo-GDP to their monophosphate form (PubMed:15850400).
In vitro, can also use dGTP, dGDP and other various nucleoside di- and triphosphates, with much lower efficiency (PubMed:1851162, PubMed:1309939, PubMed:15850400).
Works cooperatively with MutM and MutY to prevent accumulation in the DNA of oxidized guanine residues (PubMed:7739614).
6 PublicationsCatalytic activityi
- EC:3.6.1.553 Publications
Cofactori
Kineticsi
- KM=0.058 µM for 8-oxo-dGDP1 Publication
- KM=0.081 µM for 8-oxo-dGTP1 Publication
- KM=0.48 µM for 8-oxo-dGTP1 Publication
- KM=0.045 µM for 8-oxo-GDP1 Publication
- KM=0.26 µM for 8-oxo-GTP1 Publication
- KM=170 µM for dGDP1 Publication
- KM=1100 µM for dGTP2 Publications
- KM=1500 µM for dGTP1 Publication
- KM=2200 µM for dCTP1 Publication
- KM=1700 µM for dCTP1 Publication
- KM=1800 µM for dTTP1 Publication
- KM=350 µM for GDP1 Publication
- KM=1000 µM for GTP1 Publication
- KM=1200 µM for GTP1 Publication
- Vmax=3.7 pmol/min/ng enzyme toward 8-oxo-dGDP1 Publication
- Vmax=20 pmol/min/ng enzyme toward 8-oxo-dGTP1 Publication
- Vmax=4.8 pmol/min/ng enzyme toward 8-oxo-GDP1 Publication
- Vmax=22 pmol/min/ng enzyme toward 8-oxo-GTP1 Publication
- Vmax=5.9 pmol/min/ng enzyme toward dGDP1 Publication
- Vmax=44 pmol/min/ng enzyme toward dGTP1 Publication
- Vmax=3.5 pmol/min/mg enzyme toward GDP1 Publication
- Vmax=24 pmol/min/mg enzyme toward GTP1 Publication
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 23 | 8-oxo-dGTP1 Publication | 1 | |
Binding sitei | 28 | 8-oxo-dGTP1 Publication | 1 | |
Metal bindingi | 37 | Magnesium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 57 | Magnesium1 Publication | 1 | |
Binding sitei | 119 | 8-oxo-dGTP2 Publications | 1 |
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: GO_Central
- DNA replication Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase, Mutator protein |
Biological process | DNA damage, DNA repair, DNA replication |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10626-MONOMER |
BRENDAi | 3.6.1.55, 2026 |
SABIO-RKi | P08337 |
Names & Taxonomyi
Protein namesi | Recommended name: 8-oxo-dGTP diphosphatase (EC:3.6.1.553 Publications)Short name: 8-oxo-dGTPase Alternative name(s): 7,8-dihydro-8-oxoguanine-triphosphatase Mutator protein MutT dGTP pyrophosphohydrolase |
Gene namesi | Name:mutT1 Publication Ordered Locus Names:b0099, JW0097 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Chemistry databases
DrugBanki | DB02023, 8-oxo-dGMP |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000056943 | 1 – 129 | 8-oxo-dGTP diphosphataseAdd BLAST | 129 |
Proteomic databases
jPOSTi | P08337 |
PaxDbi | P08337 |
PRIDEi | P08337 |
Interactioni
Subunit structurei
Monomer.
1 PublicationBinary interactionsi
P08337
With | #Exp. | IntAct |
---|---|---|
frdB [P0AC47] | 4 | EBI-1121389,EBI-906724 |
Protein-protein interaction databases
BioGRIDi | 4261888, 366 interactors 849225, 4 interactors |
DIPi | DIP-10288N |
IntActi | P08337, 5 interactors |
STRINGi | 511145.b0099 |
Structurei
Secondary structure
3D structure databases
BMRBi | P08337 |
SMRi | P08337 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P08337 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 129 | Nudix hydrolasePROSITE-ProRule annotationAdd BLAST | 129 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 34 – 37 | 8-oxo-dGTP binding1 Publication | 4 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 38 – 59 | Nudix boxPROSITE-ProRule annotationAdd BLAST | 22 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0494, Bacteria |
HOGENOMi | CLU_037162_19_2_6 |
InParanoidi | P08337 |
PhylomeDBi | P08337 |
Family and domain databases
InterProi | View protein in InterPro IPR003561, Mutator_MutT IPR020476, Nudix_hydrolase IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
PRINTSi | PR01401, MUTATORMUTT PR00502, NUDIXFAMILY |
SUPFAMi | SSF55811, SSF55811, 1 hit |
TIGRFAMsi | TIGR00586, mutt, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
i Sequence
Sequence statusi: Complete.
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
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 |
PIRi | A27890, MVECMT |
RefSeqi | NP_414641.1, NC_000913.3 WP_000736007.1, NZ_SSZK01000004.1 |
Genome annotation databases
EnsemblBacteriai | AAC73210; AAC73210; b0099 BAB96667; BAB96667; BAB96667 |
GeneIDi | 944824 |
KEGGi | ecj:JW0097 eco:b0099 |
PATRICi | fig|1411691.4.peg.2181 |
Similar proteinsi
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 |
PIRi | A27890, MVECMT |
RefSeqi | NP_414641.1, NC_000913.3 WP_000736007.1, NZ_SSZK01000004.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1MUT | NMR | - | A | 1-129 | [»] | |
1PPX | NMR | - | A | 1-129 | [»] | |
1PUN | NMR | - | A | 1-129 | [»] | |
1PUQ | NMR | - | A | 1-129 | [»] | |
1PUS | NMR | - | A | 1-129 | [»] | |
1TUM | NMR | - | A | 1-129 | [»] | |
3A6S | X-ray | 1.80 | A/B | 1-129 | [»] | |
3A6T | X-ray | 1.96 | A | 1-129 | [»] | |
3A6U | X-ray | 2.56 | A | 1-129 | [»] | |
3A6V | X-ray | 2.00 | A/B | 1-129 | [»] | |
BMRBi | P08337 | |||||
SMRi | P08337 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261888, 366 interactors 849225, 4 interactors |
DIPi | DIP-10288N |
IntActi | P08337, 5 interactors |
STRINGi | 511145.b0099 |
Chemistry databases
DrugBanki | DB02023, 8-oxo-dGMP |
Proteomic databases
jPOSTi | P08337 |
PaxDbi | P08337 |
PRIDEi | P08337 |
Genome annotation databases
EnsemblBacteriai | AAC73210; AAC73210; b0099 BAB96667; BAB96667; BAB96667 |
GeneIDi | 944824 |
KEGGi | ecj:JW0097 eco:b0099 |
PATRICi | fig|1411691.4.peg.2181 |
Organism-specific databases
EchoBASEi | EB0621 |
Phylogenomic databases
eggNOGi | COG0494, Bacteria |
HOGENOMi | CLU_037162_19_2_6 |
InParanoidi | P08337 |
PhylomeDBi | P08337 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10626-MONOMER |
BRENDAi | 3.6.1.55, 2026 |
SABIO-RKi | P08337 |
Miscellaneous databases
EvolutionaryTracei | P08337 |
PROi | PR:P08337 |
Family and domain databases
InterProi | View protein in InterPro IPR003561, Mutator_MutT IPR020476, Nudix_hydrolase IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
PRINTSi | PR01401, MUTATORMUTT PR00502, NUDIXFAMILY |
SUPFAMi | SSF55811, SSF55811, 1 hit |
TIGRFAMsi | TIGR00586, mutt, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MUTT_ECOLI | |
Accessioni | P08337Primary (citable) accession number: P08337 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
Last sequence update: | August 1, 1988 | |
Last modified: | February 23, 2022 | |
This is version 185 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families