A0A455UBK1 · A0A455UBK1_9GAMM
- ProteinPhospholipase A1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids343 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
Cofactor
Note: Binds 1 Ca2+ ion per monomer. In the dimeric form the Ca2+ is bound by different amino acids with binding of each Ca2+ shared with ligands coming from each monomer. The Ca2+ ion may have a role in catalysis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 169 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: S | ||||||
Active site | 205 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 207 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 210 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: R | ||||||
Binding site | 215 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: S | ||||||
Binding site | 250 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell outer membrane | |
Molecular Function | 1-acyl-2-lysophosphatidylserine acylhydrolase activity | |
Molecular Function | calcium ion binding | |
Molecular Function | phosphatidylserine 1-acylhydrolase activity | |
Molecular Function | phospholipase A1 activity | |
Molecular Function | phospholipase A2 activity | |
Biological Process | lipid catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipase A1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Vreelandella
Accessions
- Primary accessionA0A455UBK1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell outer membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Note: One of the very few enzymes located there.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MVTRKLPFTKLIILLSFATFSADAFA | ||||||
Chain | PRO_5019610558 | 27-343 | Phospholipase A1 | |||
Sequence: ASQQEIEERIRALNAELYDLHQQLQRVESPEDAAQGVPFEPLPEEAAREDLSERRELEQESSRNPFSITTHRTNYLFPVSFNANKNRESFRNISGDGEVSSVELKFQFSAKVNLIEEVFGNYGDVYFGYTQRSWWQAYNTDASSPFRETNYEPEVFIDFDNAWGALGWVNTRNRVALNHQSNGRSDPLSRSWNRVYLESTFQRGDWAFTLAPHWRIPESSEDDDNPDIERYMGYGDIRLAKRLNNNHEVSGLLRGNPSAGNIGTQIDYSWPAFNSLRAHVQYYYGYGESMIDYDHRVHRLSLGFSLNPLFSATGLNR |
Interaction
Subunit
Homodimer; dimerization is reversible, and the dimeric form is the active one.
Structure
Family & Domains
Features
Showing features for coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 22-49 | |||||
Sequence: ADAFAASQQEIEERIRALNAELYDLHQQ | ||||||
Region | 55-90 | Disordered | ||||
Sequence: SPEDAAQGVPFEPLPEEAAREDLSERRELEQESSRN | ||||||
Compositional bias | 69-87 | Basic and acidic residues | ||||
Sequence: PEEAAREDLSERRELEQES |
Sequence similarities
Belongs to the phospholipase A1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length343
- Mass (Da)39,531
- Last updated2019-06-05 v1
- Checksum2EF13941A5A61298
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 69-87 | Basic and acidic residues | ||||
Sequence: PEEAAREDLSERRELEQES |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP019514 EMBL· GenBank· DDBJ | BBI62967.1 EMBL· GenBank· DDBJ | Genomic DNA |