A0QUZ2 · MUTT1_MYCS2
- Protein8-oxo-(d)GTP phosphatase
- GenemutT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids322 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-oxo-GTP to 8-oxo-GDP (PubMed:16585780, PubMed:28375146).
At high enzyme concentrations, can also catalyze the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP (PubMed:28375146).
In addition, catalyzes the hydrolysis of the diadenosine polyphosphates diadenosine hexaphosphate (Ap6A), diadenosine pentaphosphate (Ap5A) and diadenosine tetraphosphate (Ap4A) (PubMed:28705712).
At high enzyme concentrations, can also catalyze the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP (PubMed:28375146).
In addition, catalyzes the hydrolysis of the diadenosine polyphosphates diadenosine hexaphosphate (Ap6A), diadenosine pentaphosphate (Ap5A) and diadenosine tetraphosphate (Ap4A) (PubMed:28705712).
Catalytic activity
- 8-oxo-dGTP + H2O = 8-oxo-dGDP + phosphate + H+
Cofactor
Note: Can also use Mn2+, with lower efficiency.
Activity regulation
Ap4A hydrolysis is inhibited by fluoride ions.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 55-58 | substrate | ||||
Sequence: RPRY | ||||||
Binding site | 60 | substrate | ||||
Sequence: D | ||||||
Binding site | 65 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 65-67 | substrate | ||||
Sequence: KGK | ||||||
Binding site | 81 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 85 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 85 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 101 | substrate | ||||
Sequence: Y | ||||||
Binding site | 108 | substrate | ||||
Sequence: K | ||||||
Binding site | 127 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 127 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 127 | substrate | ||||
Sequence: E | ||||||
Binding site | 145 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity | |
Molecular Function | 8-oxo-dGDP phosphatase activity | |
Molecular Function | 8-oxo-GDP phosphatase activity | |
Molecular Function | metal ion binding | |
Biological Process | DNA repair | |
Biological Process | DNA replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name8-oxo-(d)GTP phosphatase
- EC number
- Short names8-oxo-(d)GTPase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionA0QUZ2
- Secondary accessions
Proteomes
Phenotypes & Variants
Disruption phenotype
12-fold spontaneous mutation frequency increase by rifampicin resistance screening.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000449349 | 1-322 | 8-oxo-(d)GTP phosphatase | |||
Sequence: MMPVDDLQEIPLSKDTTEKSKHTVRAAGAVLWRDASEHGGTTGHPATVEVAVIHRPRYDDWSLPKGKLDQGETEPVAAAREIHEETGHTAVLGRRLGRVTYPIPQGTKRVWYWAAKSTGGDFSPNDEVDKLVWLPVDAAMDQLQYPDDRKVLRRFVKRPVDTKTVLVVRHGTAGRRSRYKGDDRKRPLDKRGRAQAEALVAQLMAFGATTLYAADRVRCHQTIEPLAQELDQLIHNEPLLTEEAYAADHKAARKRLLEIAGRPGNPVICTQGKVIPGLIEWWCERAKVRPETTGNRKGSTWVLSLSDGELVGADYLSPPDEK |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MMPVDDLQEIPLSKDTTEKSK | ||||||
Domain | 22-156 | Nudix hydrolase | ||||
Sequence: HTVRAAGAVLWRDASEHGGTTGHPATVEVAVIHRPRYDDWSLPKGKLDQGETEPVAAAREIHEETGHTAVLGRRLGRVTYPIPQGTKRVWYWAAKSTGGDFSPNDEVDKLVWLPVDAAMDQLQYPDDRKVLRRFV | ||||||
Motif | 66-87 | Nudix box | ||||
Sequence: GKLDQGETEPVAAAREIHEETG |
Domain
Contains an N-terminal Nudix hydrolase domain, followed by a linker region and a C-terminal histidine phosphatase domain. The C-terminal domain is necessary for efficient catalysis by the Nudix hydrolase domain.
Sequence similarities
Belongs to the Nudix hydrolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length322
- Mass (Da)35,923
- Last updated2007-01-09 v1
- ChecksumEC7AC99FBF4D351E
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000480 EMBL· GenBank· DDBJ | ABK74793.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001663 EMBL· GenBank· DDBJ | AFP38798.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |