A8QPD8 · CUTI1_TRIHA
- ProteinCutinase cut1
- Genecut1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids248 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18987860).
May degrade cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18987860).
May also degrade suberin, a specialized macromolecule found in the cell wall of various plant tissues (PubMed:18987860).
May degrade cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18987860).
May also degrade suberin, a specialized macromolecule found in the cell wall of various plant tissues (PubMed:18987860).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.33 mM | p-nitrophenyl acetate | 8 | 25 | |||
0.57 mM | p-nitrophenyl butyrate | 8 | 25 | |||
0.82 mM | p-nitrophenyl valerate | 8 | 25 | |||
0.085 mM | p-nitrophenyl palmitate | 8 | 37 |
pH Dependence
Optimum pH is 7.5-8.
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 90 | Transition state stabilizer | ||||
Sequence: T | ||||||
Active site | 164 | Nucleophile | ||||
Sequence: S | ||||||
Site | 165 | Transition state stabilizer | ||||
Sequence: Q | ||||||
Active site | 216 | |||||
Sequence: D | ||||||
Active site | 229 | Proton donor/acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | cutinase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCutinase cut1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionA8QPD8
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MRSLSLFTALLAGQAFA | ||||||
Chain | PRO_5005117511 | 18-248 | Cutinase cut1 | |||
Sequence: YPKPVLQSSTRRDWPTINEFLTELAEIMPIGDTVSAACDLIGDAEDVAADLFDISNTENDACGDVTVLFARGTCDPGNVGVLVGPWFFNSLETALPNKKVGVKGVPYPASVQGFLSGSVQPGIDMANQIKSVISSCPNTKLVLGGYSQGSMVVHNAASNLDAATMAKVSAVVLFGDPYDGRPVANYDASKVLVVCHDGDNICQGGDFILLPHLTYAEDADTAAAFVKPLVS | ||||||
Disulfide bond | 79↔153 | |||||
Sequence: CGDVTVLFARGTCDPGNVGVLVGPWFFNSLETALPNKKVGVKGVPYPASVQGFLSGSVQPGIDMANQIKSVISSC | ||||||
Disulfide bond | 212↔219 | |||||
Sequence: CHDGDNIC |
Post-translational modification
The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme.
Keywords
- PTM
Expression
Induction
Induced during growth on olive oil (PubMed:18987860).
Induced during growth on the lipidic carbon source 16-hydroxyhexadecanoic acid (synthetic cutin monomer) (PubMed:18987860).
Induced during growth on plant material (PubMed:18987860).
Induced during growth on pectin (PubMed:18987860).
Repressed during growth on glucose carbon source (PubMed:18987860).
Induced during growth on the lipidic carbon source 16-hydroxyhexadecanoic acid (synthetic cutin monomer) (PubMed:18987860).
Induced during growth on plant material (PubMed:18987860).
Induced during growth on pectin (PubMed:18987860).
Repressed during growth on glucose carbon source (PubMed:18987860).
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length248
- Mass (Da)26,007
- Last updated2008-01-15 v1
- Checksum3CDEF12D896F9DE6