D4Q9N1 · PETH1_THEAE
- ProteinCutinase est1
- Geneest1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids296 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:25910960).
Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:25910960).
Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25910960).
Can also depolymerize the synthetic polyester poly(epsilon-caprolactone) (PCL) (PubMed:25910960).
Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:25910960).
Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25910960).
Can also depolymerize the synthetic polyester poly(epsilon-caprolactone) (PCL) (PubMed:25910960).
Catalytic activity
- (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H+This reaction proceeds in the forward direction.
(ethylene terephthalate)(n) RHEA-COMP:12420 + CHEBI:15377 = (ethylene terephthalate)(n-1) RHEA-COMP:12421 + CHEBI:131704 + CHEBI:15378 - a butanoate ester + H2O = an aliphatic alcohol + butanoate + H+This reaction proceeds in the forward direction.
Biotechnology
Has potential for application in biological recycling of plastic waste products.
pH Dependence
Optimum pH is 6.
Temperature Dependence
Optimum temperature is 50 degrees Celsius.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 95 | poly(ethylene terephthalate) (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 165 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 166 | poly(ethylene terephthalate) (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 190 | poly(ethylene terephthalate) (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Active site | 211 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 243 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | periplasmic space | |
Molecular Function | cutinase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCutinase est1
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Streptosporangiales > Nocardiopsaceae > Thermobifida
Accessions
- Primary accessionD4Q9N1
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 64 | Increases thermostability and activity on pNP-butyrate; when associated with P-249. | ||||
Sequence: A → V | ||||||
Mutagenesis | 249 | Increases thermostability and activity on pNP-butyrate; when associated with V-64. | ||||
Sequence: T → P |
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-35 | |||||
Sequence: MSVTTPRREASLLSRAVAVAAAAAATVALAAPAQA | ||||||
Chain | PRO_5003062113 | 36-296 | Cutinase est1 | |||
Sequence: ANPYERGPNPTESMLEARSGPFSVSEERASRLGADGFGGGTIYYPRENNTYGAIAISPGYTGTQSSIAWLGERIASHGFVVIAIDTNTTLDQPDSRARQLNAALDYMLTDASSSVRNRIDASRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKSWRDITVPTLIIGADLDTIAPVSSHSEPFYNSIPSSTDKAYLELNNATHFAPNITNKTIGMYSVAWLKRFVDEDTRYTQFLCPGPRTGLLSDVDEYRSTCPF | ||||||
Disulfide bond | 276↔294 | |||||
Sequence: CPGPRTGLLSDVDEYRSTC |
Keywords
- PTM
Expression
Induction
Expression is not induced by the synthetic polyester poly(butylene succinate-co-adipate) (PBSA).
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length296
- Mass (Da)31,787
- Last updated2011-09-21 v2
- Checksum997F11B4DDDF086F