A0A2I0MH85 · A0A2I0MH85_COLLI

  • Protein
    N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
  • Gene
    NAPEPLD
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

Caution

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

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 site206Zn2+ 1 (UniProtKB | ChEBI)
Binding site208Zn2+ 1 (UniProtKB | ChEBI)
Binding site209N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI)
Binding site210Zn2+ 2 (UniProtKB | ChEBI)
Binding site211Zn2+ 2 (UniProtKB | ChEBI)
Binding site274Zn2+ 1 (UniProtKB | ChEBI)
Binding site277deoxycholate (UniProtKB | ChEBI)
Binding site281deoxycholate (UniProtKB | ChEBI)
Binding site305Zn2+ 1 (UniProtKB | ChEBI)
Binding site305Zn2+ 2 (UniProtKB | ChEBI)
Binding site342N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI)
Binding site364Zn2+ 2 (UniProtKB | ChEBI)
Binding site369deoxycholate (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

    • Name
      NAPEPLD
    • ORF names
      A306_00007112

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Columbiformes > Columbidae > Columba

Accessions

  • Primary accession
    A0A2I0MH85

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region18-63Disordered
Compositional bias39-63Basic and acidic residues
Domain165-365Metallo-beta-lactamase

Sequence similarities

Belongs to the NAPE-PLD family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    414
  • Mass (Da)
    47,786
  • Last updated
    2018-02-28 v1
  • Checksum
    4C277A8A87812E0A
MLVQEKIDEFKICFSSPQKDMDKKKDEEQPLTACNQYPKEAVRKRHNSGRGSRGSDSSRSSRKSFRLDYRLEEDVTKSKRGKDGKFVNPWPTWKPPTLPNILKWSLMEKNNSNVPCSKQELDKELPVLKPYFVQKPELAGKTGPGMRVTWLGHASLMVEMDELIFLTDPIFSQRASPTQLMGPKRFRGPPCTVEQLPKIDAVVISHNHYDHLDYNTVRSLNGRFGSELRWFVPLGLLDWMQRCGCENVIELDWWEENCVPGHDAVTFVFTPSQHWCKRTATDDNKVLWGSWSVLGPWNRFFFSGDTGYCVAFEQIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHIDVQAKKSVAIHWGTFALANEYYLDPPVKLNEALERYGLKKEDFFVLNHGESRDLSTNDGFE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias39-63Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AKCR02000012
EMBL· GenBank· DDBJ
PKK29036.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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