| IED ID | IndEnz0010001199 |
| Enzyme Type ID | esterase001199 |
| Protein Name |
Cutinase EC 3.1.1.74 KrCUT |
| Gene Name | cut Krad_4111 YP_001363838.1 |
| Organism | Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Kineosporiales Kineosporiaceae Kineococcus Kineococcus radiotolerans Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) |
| Enzyme Sequence | MLRARPSHRLASAAAVVAATGAALLAGSSPAAAATCSDVDVVFARGTGETPGLGVVGGPFVRSLTGELSDRTVTSHAVDYAASSSQASAGPGATAMSAHVREVAAACPSTRFVLGGYSQGATVTDIALGIRTGTTTGTPVPAELAGRVAAVVVFGNPLGLSGRTIATASSTYGPKSKDYCNSSDSVCGSAPKTGTGGHLSYASNGSTTDGARFAAGLVRAAGTPTTPTPTPTPTPVPTTCVRDSTRDHVAADRAVSLYGRAYARGSRDSLGATSSYNVVSLQQVEGGWRLVTAC |
| Enzyme Length | 294 |
| Uniprot Accession Number | A6WFI5 |
| Absorption | |
| Active Site | ACT_SITE 118; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O53581; ACT_SITE 184; /evidence=ECO:0000250|UniProtKB:O53581; ACT_SITE 198; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:O53581 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:34705546}; 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:34705546};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47389; Evidence={ECO:0000269|PubMed:34705546}; 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:34705546};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393; Evidence={ECO:0000269|PubMed:34705546}; 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:34705546};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:34705546}; 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:34705546}; |
| DNA Binding | |
| EC Number | 3.1.1.74 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:34705546). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:34705546). Can depolymerize synthetic polyesters such as poly(epsilon-caprolactone) (PCL) and poly(1,3-propylene adipate) (PPA) (PubMed:34705546). Exhibits some activity on poly(lactic acid) (PLA) (PubMed:34705546). Can bind but not hydrolyze poly(hydroxybutyrate) (PHB) (PubMed:34705546). {ECO:0000269|PubMed:34705546}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:34705546}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Region (2); Signal peptide (1); Site (1) |
| Keywords | Disulfide bond;Hydrolase;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:34705546}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000305|PubMed:34705546 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,136 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:47388; RHEA:47389; RHEA:47392; RHEA:47393; RHEA:47348; RHEA:47349; RHEA:47356 |
| Cross Reference Brenda |