| IED ID | IndEnz0010000997 |
| Enzyme Type ID | esterase000997 |
| Protein Name |
Cutinase cut1 EC 3.1.1.74 Poly ethylene terephthalate hydrolase PET hydrolase PETase EC 3.1.1.101 |
| Gene Name | cut_1 |
| Organism | Thermobifida fusca (Thermomonospora fusca) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptosporangiales Nocardiopsaceae Thermobifida Thermobifida fusca (Thermomonospora fusca) |
| Enzyme Sequence | MPPHAARPGPAQNRRGRAMAVITPRRERSSLLSRALRFTAAAATALVTAVSLAAPAHAANPYERGPNPTDALLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAVAISPGYTGTQASVAWLGERIASHGFVVITIDTNTTLDQPDSRARQLNAALDYMINDASSAVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVRVPTLIIGADLDTIAPVLTHARPFYNSLPTSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF |
| Enzyme Length | 319 |
| Uniprot Accession Number | G8GER6 |
| Absorption | |
| Active Site | ACT_SITE 188; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; ACT_SITE 234; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7; ACT_SITE 266; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:A0A0K8P6T7 |
| Activity Regulation | ACTIVITY REGULATION: Activated by magnesium ions (PubMed:25545638). Activated by calcium ions (PubMed:25545638). {ECO:0000269|PubMed:25545638}. |
| Binding Site | BINDING 118; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:F7IX06; BINDING 189; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:F7IX06; BINDING 213; /note=Poly(ethylene terephthalate); /evidence=ECO:0000250|UniProtKB:F7IX06 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:25545638};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:25545638}; CATALYTIC ACTIVITY: Reaction=H2O + pentanoate ester = an aliphatic alcohol + H(+) + pentanoate; Xref=Rhea:RHEA:48436, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31011, ChEBI:CHEBI:50871; Evidence={ECO:0000269|PubMed:23604968};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48437; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658; Evidence={ECO:0000269|PubMed:23604968};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47361; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:23604968};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47365; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:23604968};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47389; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:23604968};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+); Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701, ChEBI:CHEBI:131704; EC=3.1.1.101; Evidence={ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:32269349};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529; Evidence={ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:32269349}; |
| DNA Binding | |
| EC Number | 3.1.1.74; 3.1.1.101 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Probable). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:23604968, PubMed:25545638). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25545638, PubMed:32269349). {ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:32269349, ECO:0000305|PubMed:23604968}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius (PubMed:23604968). Optimum temperature is 65 degrees Celsius (PubMed:32269349). {ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:32269349}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:23604968}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (3); Chain (1); Disulfide bond (1); Signal peptide (1) |
| Keywords | Disulfide bond;Hydrolase;Periplasm;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23604968}. Periplasm {ECO:0000269|PubMed:23604968}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..58; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,422 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=131 uM for pNP-butanoate (at 50 degrees Celsius and pH 8) {ECO:0000269|PubMed:23604968}; Note=kcat is 178 sec(-1) for the hydrolysis of pNP-butanoate (at 50 degrees Celsius and pH 8). {ECO:0000269|PubMed:23604968}; |
| Metal Binding | |
| Rhea ID | RHEA:12957; RHEA:47348; RHEA:47349; RHEA:48436; RHEA:48437; RHEA:47356; RHEA:47360; RHEA:47361; RHEA:47364; RHEA:47365; RHEA:47388; RHEA:47389; RHEA:47392; RHEA:47393; RHEA:49528; RHEA:49529 |
| Cross Reference Brenda | 3.1.1.74; |