P22088 · LIP_BURCE
- ProteinTriacylglycerol lipase
- Genelip
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids364 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the hydrolysis of triacylglycerol. It shows a preference for triacylglycerols with a chain length between 6 and 12 carbons.
Catalytic activity
- a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Activity regulation
Inhibited by RC-(Rp,Sp)- and SC-(Rp,Sp)-1,2-dioctylcarbamoylglycero-3-O-p-nitrophenyl octylphosphonate (PubMed:9660188).
Also inhibited by diethyl-p-nitrophenylphosphate (E600) (PubMed:1856176).
Also inhibited by diethyl-p-nitrophenylphosphate (E600) (PubMed:1856176).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 61 | substrate | ||||
Sequence: L | ||||||
Active site | 131 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 132 | substrate | ||||
Sequence: Q | ||||||
Binding site | 286 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 308 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 330 | Charge relay system | ||||
Sequence: H | ||||||
Binding site | 332 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 336 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 340 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | metal ion binding | |
Molecular Function | triglyceride lipase activity | |
Biological Process | lipid catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTriacylglycerol lipase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex
Accessions
- Primary accessionP22088
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-44 | |||||
Sequence: MARTMRSRVVAGAVACAMSIAPFAGTTAVMTLATTHAAMAATAP | ||||||
Chain | PRO_0000017740 | 45-364 | Triacylglycerol lipase | |||
Sequence: AAGYAATRYPIILVHGLSGTDKYAGVLEYWYGIQEDLQQNGATVYVANLSGFQSDDGPNGRGEQLLAYVKTVLAATGATKVNLVGHSQGGLSSRYVAAVAPDLVASVTTIGTPHRGSEFADFVQDVLAYDPTGLSSSVIAAFVNVFGILTSSSHNTNQDALAALQTLTTARAATYNQNYPSAGLGAPGSCQTGAPTETVGGNTHLLYSWAGTAIQPTLSVFGVTGATDTSTLPLVDPANVLDLSTLALFGTGTVMINRGSGQNDGLVSKCSALYGKVLSTSYKWNHLDEINQLLGVRGAYAEDPVAVIRTHANRLKLAGV | ||||||
Disulfide bond | 234↔314 | |||||
Sequence: CQTGAPTETVGGNTHLLYSWAGTAIQPTLSVFGVTGATDTSTLPLVDPANVLDLSTLALFGTGTVMINRGSGQNDGLVSKC |
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 54-266 | AB hydrolase-1 | ||||
Sequence: PIILVHGLSGTDKYAGVLEYWYGIQEDLQQNGATVYVANLSGFQSDDGPNGRGEQLLAYVKTVLAATGATKVNLVGHSQGGLSSRYVAAVAPDLVASVTTIGTPHRGSEFADFVQDVLAYDPTGLSSSVIAAFVNVFGILTSSSHNTNQDALAALQTLTTARAATYNQNYPSAGLGAPGSCQTGAPTETVGGNTHLLYSWAGTAIQPTLSVFG |
Sequence similarities
Belongs to the AB hydrolase superfamily. Pseudomonas lipase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length364
- Mass (Da)37,494
- Last updated1996-02-01 v2
- ChecksumE9CD2DBFB55658E9
Keywords
- Technical term