P9WIX9 · MUTT3_MYCTU

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

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site70Mg2+ (UniProtKB | ChEBI)
Binding site85Mg2+ (UniProtKB | ChEBI)
Binding site88Mg2+ (UniProtKB | ChEBI)
Binding site89Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
Molecular Functionmetal ion binding
Biological ProcessDNA repair
Biological ProcessDNA replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Putative 8-oxo-dGTP diphosphatase 3
  • EC number
  • Short names
    8-oxo-dGTPase
  • Alternative names
    • 7,8-dihydro-8-oxoguanine-triphosphatase 3
    • Mutator protein MutT3
    • dGTP pyrophosphohydrolase 3

Gene names

    • Name
      mutT3
    • Ordered locus names
      Rv0413

Organism names

Accessions

  • Primary accession
    P9WIX9
  • Secondary accessions
    • L0T5A7
    • P96259
    • Q7D9V1

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

No visible phenotype.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003917771-217Putative 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
IDPosition(s)Description
Domain30-164Nudix hydrolase
Region67-92Disordered
Motif70-91Nudix box
Compositional bias77-92Basic and acidic residues

Sequence similarities

Belongs to the Nudix hydrolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    217
  • Mass (Da)
    23,499
  • Last updated
    2014-04-16 v1
  • MD5 Checksum
    88629AD51D1C57BE2996293A1ECECDBD
MPSCPPAYSEQVRGDGDGWVVSDSGVAYWGRYGAAGLLLRAPRPDGTPAVLLQHRALWSHQGGTWGLPGGARDSHETPEQTAVRESSEEAGLSAERLEVRATVVTAEVCGVDDTHWTYTTVVADAGELLDTVPNRESAELRWVAENEVADLPLHPGFAASWQRLRTAPATVPLARCDERRQRLPRTIQIEAGVFLWCTPGDADQAPSPLGRRISSLL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias77-92Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL123456
EMBL· GenBank· DDBJ
CCP43144.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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