A0A0J2K8A7 · A0A0J2K8A7_9ENTR
- ProteinPhospholipase A1
- GenepldA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids290 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 127 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: S | ||||||
Active site | 163 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 165 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 168 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: R | ||||||
Binding site | 173 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: S | ||||||
Binding site | 205 | 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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella
Accessions
- Primary accessionA0A0J2K8A7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell outer 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 | 1-20 | |||||
Sequence: MRISLACLLALVALPAGVLA | ||||||
Chain | PRO_5015041187 | 21-290 | Phospholipase A1 | |||
Sequence: QDAPVNKQVHDAPVVRGSIIANLLQDHDNPFLLYPYESNYLLYTWTSDLNKEAIRSYDWAENARKDEVKFQLSLAFPLWRGILGENSLLGASYTQKSWWQLSNSKESAPFRETNYEPQLFLGFATDYSFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAQNGNWLVEVKPWYVIGSTDDNPDITKYMGYYRLKVGYQLGDAILSAQGQYNWNTGYGGAELGVSYPITKHVRVYTQVYSGYGESLIDYNFNQTRVGVGLMLNDLF |
Interaction
Subunit
Homodimer; dimerization is reversible, and the dimeric form is the active one.
Structure
Sequence
- Sequence statusComplete
- Length290
- Mass (Da)33,018
- Last updated2017-03-15 v1
- Checksum8758F584E711229D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JCNZ01000003 EMBL· GenBank· DDBJ | EWF93906.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAOCBF010000025 EMBL· GenBank· DDBJ | MDH0964794.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JASUWR010000001 EMBL· GenBank· DDBJ | MDL4488313.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
PIET01000054 EMBL· GenBank· DDBJ | PLM67998.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
PIDR01000102 EMBL· GenBank· DDBJ | PLO73461.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP048108 EMBL· GenBank· DDBJ | QHS47797.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QKPB01000019 EMBL· GenBank· DDBJ | RWT45194.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UGMS01000002 EMBL· GenBank· DDBJ | STW66112.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP102103 EMBL· GenBank· DDBJ | UWZ73954.1 EMBL· GenBank· DDBJ | Genomic DNA |