A0A7K9P573 · A0A7K9P573_9CORV

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • 2 H2O + ITP = 2 H+ + IMP + 2 phosphate
    This reaction proceeds in the forward direction.
  • 2 H2O + UTP = 2 H+ + 2 phosphate + UMP
    This reaction proceeds in the forward direction.
  • ADP + H2O = AMP + H+ + phosphate
    This reaction proceeds in the forward direction.
  • ATP + 2 H2O = AMP + 2 H+ + 2 phosphate
    This reaction proceeds in the forward direction.
  • ATP + H2O = ADP + H+ + phosphate
    This reaction proceeds in the forward direction.
  • CDP + H2O = CMP + H+ + phosphate
    This reaction proceeds in the forward direction.
  • CTP + 2 H2O = CMP + 2 H+ + 2 phosphate
    This reaction proceeds in the forward direction.
  • CTP + H2O = CDP + H+ + phosphate
    This reaction proceeds in the forward direction.
  • GDP + H2O = GMP + H+ + phosphate
    This reaction proceeds in the forward direction.
  • GTP + 2 H2O = GMP + 2 H+ + 2 phosphate
    This reaction proceeds in the forward direction.
  • H2O + IDP = H+ + IMP + phosphate
    This reaction proceeds in the forward direction.
  • H2O + ITP = H+ + IDP + phosphate
    This reaction proceeds in the forward direction.
  • H2O + UDP = H+ + phosphate + UMP
    This reaction proceeds in the forward direction.
  • H2O + UTP = H+ + phosphate + UDP
    This reaction proceeds in the forward direction.
  • a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H+ + phosphate
    This reaction proceeds in the forward direction.
  • a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H+ + 2 phosphate
    This reaction proceeds in the forward direction.
    EC:3.6.1.5 (UniProtKB | ENZYME | Rhea)
  • a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphate
    This reaction proceeds in the forward direction.

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site157Proton acceptor
Binding site199-203ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular Functionhydrolase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ectonucleoside triphosphate diphosphohydrolase 1
  • EC number
  • Alternative names
    • ATP diphosphohydrolase
    • Ecto-ATP diphosphohydrolase 1
    • Ecto-apyrase
    • Lymphoid cell activation antigen
    • Nucleoside triphosphate diphosphohydrolase 1

Gene names

    • Name
      Entpd1
    • ORF names
      PACPHI_R11698

Organism names

  • Taxonomic identifier
  • Strain
    • B10K-DU-001-28
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Passeriformes > Corvoidea > Pachycephalidae > Pachycephala

Accessions

  • Primary accession
    A0A7K9P573

Proteomes

Subcellular Location

Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane465-487Helical

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_502951872120-498Ectonucleoside triphosphate diphosphohydrolase 1

Interaction

Subunit

Homodimer; disulfide-linked.

Family & Domains

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    498
  • Mass (Da)
    55,356
  • Last updated
    2021-04-07 v1
  • Checksum
    41D7760E4449A3ED
LLILGFLSTLAVIALIAVAVTQNKPLPKNIKYGIVLDAGSSHTNLYVYEWPAEKENDTGVVKQVEVCKVEGPGISGYSHATEEAGPSLAQCLQQAKEVIPSAQHKETPVYLGATAGMRLLRLQNKSAADKVLSSVENTLRSAPFNFQGARIITGQEEGAYGWITINYLLGNFKQVSGWKKLLQSLTSLSETSGALDLGGASTQITFVSKDLSSESPENQLYFRLYGKDYQVYTHSFLCYGKDQALQQKLARDLQASTSTPSSSLLDPCFHQGYQRTINISEFFKNPCTSDKKKELPFSQLYIEGEGDYQKCRENIQTLFNKTNCPYSRCSFNGIYLPPLQGDFGAFSAFYFVMNFLNLTSEPKPLALNKVTSTIESFCARPWQEVKTAYHRVKEKYLSEYCFSGAYILSLLENGYEFTENNWQMIHFLGKIGSSDAGWTLGYMLNLTNMIPAEDPAEPPLSHGSYVGLMVLCSLVLVSVLLFAWLLFHKPKCLQKGIV

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue498

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VWZT01001037
EMBL· GenBank· DDBJ
NXH94055.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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