A0A8C0B1F9 · A0A8C0B1F9_9AVES
- ProteinN-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids394 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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-hexadecanoylethanolamineThis 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) ethanolamineThis 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-hexadecanoylethanolamineThis reaction proceeds in the forward direction.
- H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamineThis 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)-ethanolamineThis 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)-ethanolamineThis 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)-ethanolamineThis 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 ethanolamineThis 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 ethanolamineThis 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-dodecanoylethanolamineThis 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-hexadecanoylethanolamineThis 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 ethanolamineThis 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 ethanolamineThis 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 ethanolamineThis 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-tetradecanoylethanolamineThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 zinc divalent cations per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 186 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 188 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 189 | N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 190 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 191 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 254 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 257 | deoxycholate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 261 | deoxycholate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 285 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 285 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 322 | N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 344 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 349 | deoxycholate (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | early endosome membrane | |
Cellular Component | Golgi membrane | |
Molecular Function | N-acylphosphatidylethanolamine-specific phospholipase D activity | |
Molecular Function | zinc ion binding | |
Biological Process | phospholipid catabolic process |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Accipitriformes > Accipitridae > Accipitrinae > Buteo
Accessions
- Primary accessionA0A8C0B1F9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-44 | Disordered | ||||
Sequence: MDKKTDEEQPLTACNQYPKEAVRKRQNSGRGSRGSDSSRTSRKS | ||||||
Compositional bias | 23-44 | Basic and acidic residues | ||||
Sequence: RKRQNSGRGSRGSDSSRTSRKS | ||||||
Domain | 145-345 | Metallo-beta-lactamase | ||||
Sequence: FLTDPIFSQRASPTQLVGPKRFRGPPCTVEQLPKIDAVMISHTHYDHLDYNTVTSLNERFGSELRWFVPLGLLDWMQRCGCENVIELDWWEENCVPGHDAVTFVFTPSQHWCKRTATDDNKVLWGSWSVLGPWNRFFFSGDTGYCVAFEQIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHIDVQAKKSVAIHW |
Sequence similarities
Belongs to the NAPE-PLD family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length394
- Mass (Da)45,366
- Last updated2022-01-19 v1
- Checksum8BB719D5B4153180
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 23-44 | Basic and acidic residues | ||||
Sequence: RKRQNSGRGSRGSDSSRTSRKS |
Keywords
- Technical term