| IED ID | IndEnz0010001139 |
| Enzyme Type ID | esterase001139 |
| Protein Name |
4-O-methyl-glucuronoyl methylesterase 1 EC 3.1.1.117 Glucuronoyl esterase 1 GE1 |
| Gene Name | WOLCODRAFT_23632 |
| Organism | Wolfiporia cocos (strain MD-104) (Brown rot fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Laetiporaceae Wolfiporia Wolfiporia cocos Wolfiporia cocos (strain MD-104) (Brown rot fungus) |
| Enzyme Sequence | MASSSRFAALLLLALPALALPPSQVVPRAACATPSTVPGYNNDRLPDPFLFDDGTAVTSSADWDCRRSQIAAVVQGYEAGYLPPQPPIVSATFSSSDGTGTLTVTAGLSSDNTISFSEPITYPSGTAPAAGWPLVIAYDVLSIPVPDGIAVMVYNNDDIAQENDLSSRGVGLFYDLYGTDATASAMTAWVWGVSRIIDALETTPAANINTAKIAVTGCSRDGKGALMAGAFEPRVALTIPQESGSGGDTCWRLSKYEQDSGDVVQQATEIVTENVWFSTNFDNYVNNLSVLPYDHHELAAMVAPRPLLSYENTEYEWLSPLSAYGCMSAAHTVYEALGIPDYHGFVQVGNHSHCYFPDTLDDSLYAFFDRFLLDEDDVSTDYFTTNYQFNGTVWNASYWINWTTPQLD |
| Enzyme Length | 408 |
| Uniprot Accession Number | P0CU53 |
| Absorption | |
| Active Site | ACT_SITE 219; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:G2QJR6; ACT_SITE 353; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Activity Regulation | |
| Binding Site | BINDING 223; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 265; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 273; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 317; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+); Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668; EC=3.1.1.117; Evidence={ECO:0000269|PubMed:28429057};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:28429057}; |
| DNA Binding | |
| EC Number | 3.1.1.117 |
| Enzyme Function | FUNCTION: Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin. Can hydrolyze benzyl glucuronic acid (BnGlcA), allyl glucuronic acid (allylGlcA) and to a lower degree methyl glucuronic acid (MeGlcA) in vitro. {ECO:0000269|PubMed:28429057}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Disulfide bond (3); Glycosylation (5); Motif (1); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Lignin degradation;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0CT87}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 217..222; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Gene Encoded By | |
| Mass | 44,123 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 mM for benzyl glucuronic acid {ECO:0000269|PubMed:28429057}; Vmax=1.91 umol/min/mg enzyme for benzyl glucuronic acid {ECO:0000269|PubMed:28429057}; |
| Metal Binding | |
| Rhea ID | RHEA:67452; RHEA:67453 |
| Cross Reference Brenda | 3.1.1.B11; |