Function and Biology

Legionella pneumophila NTPDase1 crystal form II (closed) in complex with MG UMPPNP

Source organism: Legionella pneumophila
Biochemical function: metal ion binding
Biological process: not assigned
Cellular component: not assigned

EC 3.6.1.5: Apyrase

Reaction catalysed:
A nucleoside 5'-triphosphate + 2 H(2)O = a nucleoside 5'-phosphate + 2 phosphate.
Comments:
  • Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyze NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates.
  • They differ from ATPases, which specifically hydrolyze ATP, by hydrolyzing both ATP and ADP.
  • Most of the ecto-ATPases that occur on the cell surface and hydrolyze extracellular nucleotides belong to this enzyme family.
Systematic name:
Nucleoside triphosphate phosphohydrolase (nucleoside monophosphoate-forming)
Alternative Name(s):
  • ADPase
  • ATP diphosphohydrolase
  • ATP-diphosphatase
  • Adenosine diphosphatase
  • ATP-diphosphohydrolase

GO terms

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Sequence family

CATH Protein family (Pfam)
PF01150
Domain description: GDA1/CD39 (nucleoside phosphatase) family
Occurring in:
  1. Ectonucleoside triphosphate diphosphohydrolase I
2 copies of Pfam domain PF01150 (GDA1/CD39 (nucleoside phosphatase) family) in Ectonucleoside triphosphate diphosphohydrolase I in PDB 4bri.

CATH InterPro annotation
IPR000407
Domain description: Nucleoside phosphatase GDA1/CD39
Occurring in:
  1. Ectonucleoside triphosphate diphosphohydrolase I

Structure domain

CATH CATH domain
3.30.420.150
Class: Alpha Beta
Architecture: 2-Layer Sandwich
Topology: Nucleotidyltransferase; domain 5
Homology: Exopolyphosphatase. Domain 2
Occurring in:
  1. Ectonucleoside triphosphate diphosphohydrolase I
1 copy of CATH domain 3.30.420.150 (Nucleotidyltransferase; domain 5) in Ectonucleoside triphosphate diphosphohydrolase I in PDB 4bri.