A0A9X7YC06 · A0A9X7YC06_SPHYA
- ProteinPhospholipase A1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids415 (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 | 243 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: S | ||||||
Active site | 278 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 280 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 283 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: R | ||||||
Binding site | 288 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: S | ||||||
Binding site | 325 | Ca2+ 1 (UniProtKB | ChEBI); in dimeric form | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell outer membrane | |
Molecular Function | metal ion binding | |
Molecular Function | phospholipase 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingobium
Accessions
- Primary accessionA0A9X7YC06
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 | 1-33 | |||||
Sequence: MIDRLFARACRARVHLLLIAGTALCPTMLRAQA | ||||||
Chain | PRO_5041012755 | 34-415 | Phospholipase A1 | |||
Sequence: PVETLIGRVGATDAQGMAAIELRFLNMGAAPATMPLPDRVEALVEQDGAARRLWLRRAPGVPETVEIAPGGFAQARYQLAASDMAEGALLSIPAWNSPQVALHGAAPARMAAASPVPVPPPPPPPGTPVPPPVAPPADRSAGNAFIGNLAPYEPIYAVYGPGTNTDARLQLSFEYRLFGSRDAAHLPSSWRDGLHFAYTQRMFWDLGANSMPFRNIDYQPEIIYVTPTRMLKNGMSLALQGGLRHESNGRDGDASRSINSVYVAPMAAFSLGEERRLLVAPRLTFYVGDKSDNPDIVRYRGHAGLFLQVGDDDGLRLSTNSRFNFGSGKGAINADLSYPLPRLLGGGPDLYLFAQGFAGYGENLLDYNRSITRLRIGFALVR |
Interaction
Subunit
Homodimer; dimerization is reversible, and the dimeric form is the active one.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 145-168 | Disordered | ||||
Sequence: AASPVPVPPPPPPPGTPVPPPVAP | ||||||
Compositional bias | 146-168 | Pro residues | ||||
Sequence: ASPVPVPPPPPPPGTPVPPPVAP |
Sequence similarities
Belongs to the phospholipase A1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length415
- Mass (Da)44,762
- Last updated2023-11-08 v1
- ChecksumB7707765E61989F4
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 146-168 | Pro residues | ||||
Sequence: ASPVPVPPPPPPPGTPVPPPVAP |