A0A0G3HEM8 · A0A0G3HEM8_9CORY

Function

function

Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site7-12substrate
Active site72Proton acceptor
Binding site72Mg2+ (UniProtKB | ChEBI)
Binding site73substrate
Binding site155-158substrate
Binding site184substrate
Binding site189-190substrate

GO annotations

AspectTerm
Molecular FunctiondITP diphosphatase activity
Molecular FunctionITP diphosphatase activity
Molecular Functionmetal ion binding
Molecular Functionnucleotide binding
Molecular Functionribonucleoside triphosphate phosphatase activity
Molecular FunctionXTP diphosphatase activity
Biological Processnucleotide metabolic process
Biological Processpurine nucleoside triphosphate catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    dITP/XTP pyrophosphatase
  • EC number
  • Alternative names
    • Non-canonical purine NTP pyrophosphatase
    • Non-standard purine NTP pyrophosphatase
    • Nucleoside-triphosphate diphosphatase
    • Nucleoside-triphosphate pyrophosphatase
      (NTPase
      )

Gene names

    • ORF names
      CUTER_08850

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 45634
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium

Accessions

  • Primary accession
    A0A0G3HEM8

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region166-188Disordered

Sequence similarities

Belongs to the HAM1 NTPase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    208
  • Mass (Da)
    21,337
  • Last updated
    2015-09-16 v1
  • Checksum
    C6E8BB349FBAE7ED
MKLLVASNNSKKLAELQRILAAAGVAGVELVALNDAPRYEEPVEDGATFAENALIKARAGAAATGWPCVADDSGLSVDALGGMPGVLSARWSGTHGDDAANNALVLAQLADVPEHRRGAAFVSACALVTPTGEETVSEGRWPGRLLHSPVGENGFGYDPLFVPAEEDAPGAAGRSSAQLSREEKDALSHRGRALAGLVTTIAQMAAES

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP011546
EMBL· GenBank· DDBJ
AKK11749.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp