P9WIX9 · MUTT3_MYCTU
- ProteinPutative 8-oxo-dGTP diphosphatase 3
- GenemutT3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids217 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
May be involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) 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 (By similarity).
Miscellaneous
There are 4 mutT paralogs in M.tuberculosis; the exact function of each is unknown.
Catalytic activity
- 8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H+
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 70 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 85 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 88 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 89 | Mg2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase 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 namePutative 8-oxo-dGTP diphosphatase 3
- EC number
- Short names8-oxo-dGTPase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionP9WIX9
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
No visible phenotype.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000391777 | 1-217 | Putative 8-oxo-dGTP diphosphatase 3 | ||
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, motif, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 30-164 | Nudix hydrolase | |||
Region | 67-92 | Disordered | |||
Motif | 70-91 | Nudix box | |||
Compositional bias | 77-92 | Basic and acidic residues | |||
Sequence similarities
Belongs to the Nudix hydrolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length217
- Mass (Da)23,499
- Last updated2014-04-16 v1
- MD5 Checksum88629AD51D1C57BE2996293A1ECECDBD
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 77-92 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP43144.1 EMBL· GenBank· DDBJ | Genomic DNA |