A0QUZ2 · MUTT1_MYCS2

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).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Can also use Mn2+, with lower efficiency.

Activity regulation

Ap4A hydrolysis is inhibited by fluoride ions.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site55-58substrate
Binding site60substrate
Binding site65Mg2+ 1 (UniProtKB | ChEBI)
Binding site65-67substrate
Binding site81Mg2+ 2 (UniProtKB | ChEBI)
Binding site85Mg2+ 1 (UniProtKB | ChEBI)
Binding site85Mg2+ 2 (UniProtKB | ChEBI)
Binding site101substrate
Binding site108substrate
Binding site127Mg2+ 1 (UniProtKB | ChEBI)
Binding site127Mg2+ 2 (UniProtKB | ChEBI)
Binding site127substrate
Binding site145substrate

GO annotations

AspectTerm
Molecular Function8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
Molecular Function8-oxo-dGDP phosphatase activity
Molecular Function8-oxo-GDP phosphatase activity
Molecular Functionmetal ion binding
Biological ProcessDNA repair
Biological ProcessDNA replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    8-oxo-(d)GTP phosphatase
  • EC number
  • Short names
    8-oxo-(d)GTPase
  • Alternative names
    • 8-oxo-(d)GDP phosphatase
      (EC:3.6.1.58
      ) . EC:3.6.1.58 (UniProtKB | ENZYME | Rhea)
    • Diadenosine hexaphosphate hydrolase
      (Ap6A hydrolase
      ) (EC:3.6.1.61
      ) . EC:3.6.1.61 (UniProtKB | ENZYME | Rhea)
    • MsMutT1

Gene names

    • Name
      mutT1
    • Ordered locus names
      MSMEG_2390
      , MSMEI_2330

Organism names

Accessions

  • Primary accession
    A0QUZ2
  • Secondary accessions
    • I7FJ40

Proteomes

Phenotypes & Variants

Disruption phenotype

12-fold spontaneous mutation frequency increase by rifampicin resistance screening.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004493491-3228-oxo-(d)GTP phosphatase

Proteomic databases

Interaction

Subunit

Forms head-to-tail homodimers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, motif.

TypeIDPosition(s)Description
Region1-21Disordered
Domain22-156Nudix hydrolase
Motif66-87Nudix box

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 status
    Complete
  • Length
    322
  • Mass (Da)
    35,923
  • Last updated
    2007-01-09 v1
  • Checksum
    EC7AC99FBF4D351E
MMPVDDLQEIPLSKDTTEKSKHTVRAAGAVLWRDASEHGGTTGHPATVEVAVIHRPRYDDWSLPKGKLDQGETEPVAAAREIHEETGHTAVLGRRLGRVTYPIPQGTKRVWYWAAKSTGGDFSPNDEVDKLVWLPVDAAMDQLQYPDDRKVLRRFVKRPVDTKTVLVVRHGTAGRRSRYKGDDRKRPLDKRGRAQAEALVAQLMAFGATTLYAADRVRCHQTIEPLAQELDQLIHNEPLLTEEAYAADHKAARKRLLEIAGRPGNPVICTQGKVIPGLIEWWCERAKVRPETTGNRKGSTWVLSLSDGELVGADYLSPPDEK

Sequence caution

The sequence AFP38798.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000480
EMBL· GenBank· DDBJ
ABK74793.1
EMBL· GenBank· DDBJ
Genomic DNA
CP001663
EMBL· GenBank· DDBJ
AFP38798.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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