A0A094KY37 · A0A094KY37_ANTCR

Function

Catalytic activity

  • 1-O-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H2O = 1-O-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N,1,2-tri-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-(9Z-octadecenoyl) ethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-3-phosphate + an N-acylethanolamine + H+
    This reaction proceeds in the forward direction.
  • H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-butanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-butanoyl ethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-decanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-decanoyl ethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-dodecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-dodecanoylethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-hexanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-hexanoyl ethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-octadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-octadecanoyl ethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-octanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-octanoyl ethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N-tetradecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-tetradecanoylethanolamine
    This reaction proceeds in the forward direction.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 zinc divalent cations per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site192Zn2+ 1 (UniProtKB | ChEBI)
Binding site194Zn2+ 1 (UniProtKB | ChEBI)
Binding site195N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI)
Binding site196Zn2+ 2 (UniProtKB | ChEBI)
Binding site197Zn2+ 2 (UniProtKB | ChEBI)
Binding site260Zn2+ 1 (UniProtKB | ChEBI)
Binding site263deoxycholate (UniProtKB | ChEBI)
Binding site267deoxycholate (UniProtKB | ChEBI)
Binding site291Zn2+ 1 (UniProtKB | ChEBI)
Binding site291Zn2+ 2 (UniProtKB | ChEBI)
Binding site328N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI)
Binding site350Zn2+ 2 (UniProtKB | ChEBI)
Binding site355deoxycholate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentearly endosome membrane
Cellular ComponentGolgi membrane
Molecular FunctionN-acylphosphatidylethanolamine-specific phospholipase D activity
Molecular Functionzinc ion binding
Biological Processphospholipid catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
  • EC number

Gene names

    • ORF names
      N321_12954

Organism names

Accessions

  • Primary accession
    A0A094KY37

Proteomes

Subcellular Location

Early endosome membrane
; Peripheral membrane protein
Golgi apparatus membrane
; Peripheral membrane protein

Interaction

Subunit

Homodimer. Bile acids promote the assembly of inactive monomers into an active dimer and enable catalysis.

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-15Basic and acidic residues
Region1-49Disordered
Compositional bias29-49Basic and acidic residues
Domain151-351Metallo-beta-lactamase

Sequence similarities

Belongs to the NAPE-PLD family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    400
  • Mass (Da)
    46,023
  • Last updated
    2014-11-26 v1
  • Checksum
    3A6689C2C827C091
SSPQKDMDKKTDEEQPLTTCNQYPKEAVRKRQNSGRGSRGSDSSRASRKSFRLDYRLEEDVTKSKRGKDGKFVNPWPTWKSPTLPNILKWSLMEKNNSNVPCSKQELDKELPVLKPYFVQKPELAGKTGTGMRVTWLGHASVMVEMDELIFLTDPIFSQRASPTQLVGPKRFRGPPCTVEQLPKIDAVMISHTHYDHLDYNTVTSLNERFGSELRWFVPLGLLDWMQRCGCENVIELDWWEENCVPGHDAVTFVFTPSQHWCKRTATDDNKVLWGSWSVLGPWNRFFFSGDTGYCLAFEQIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHIDVQAKKSVAIHWGTFALANEYYLDPPVKLNEALERYGLKKEDFFVLNHGESRDLSTNDGFD

Features

Showing features for non-terminal residue, compositional bias.

TypeIDPosition(s)Description
Non-terminal residue1
Compositional bias1-15Basic and acidic residues
Compositional bias29-49Basic and acidic residues
Non-terminal residue400

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KL358899
EMBL· GenBank· DDBJ
KFZ64058.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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