IED ID | IndEnz0010001144 |
Enzyme Type ID | esterase001144 |
Protein Name |
4-O-methyl-glucuronoyl methylesterase EC 3.1.1.117 Glucuronoyl esterase GE |
Gene Name | |
Organism | Cerrena unicolor (Canker rot fungus) (Daedalea unicolor) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Cerrenaceae Cerrena Cerrena unicolor (Canker rot fungus) (Daedalea unicolor) |
Enzyme Sequence | MFKPSFVALALVSYATAQASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCLQGAAPAPARTTAAPPPPPATTAAPPPPTTSAPTGSSPVAGACGAIASTVPNYNNAKLPDPFTFANGTALRTKADWSCRRAEISALIQNYEAGTLPPKPPVVTASFSKSGNTGTLAITAGLSNSQTIKFSPTISYPSGTPPANGWPLIIAYEGGSIPIPAGVATLTYSNSDMAQQNSASSRGQGLFYQLYGSTHSASAMTAWVWGVSRIIDALEMTPTAQINTQRIGVTGCSRDGKGALMAGAFEERIALTIPQESGSGGDACWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPEDHHLLAAMVAPRAMISFENTDYLWLSPMSSFGCMTAAHTVWQGLGIADSHGFAQVGGHAHCAWPSSLTPQLNAFINRFLLDQSATTNVFTTNNQFGKVQWNAANWITWTTPTLT |
Enzyme Length | 474 |
Uniprot Accession Number | A0A0A7EQR3 |
Absorption | |
Active Site | ACT_SITE 286; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:G2QJR6; ACT_SITE 420; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
Activity Regulation | |
Binding Site | BINDING 290; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 332; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 340; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 384; /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:25425346, ECO:0000269|PubMed:26712478};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:25425346, ECO:0000305|PubMed:26712478}; |
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 (PubMed:25425346, PubMed:26712478). {ECO:0000269|PubMed:25425346, ECO:0000269|PubMed:26712478}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (11); Binding site (4); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (18); Motif (1); Region (1); Signal peptide (1); Turn (3) |
Keywords | 3D-structure;Disulfide bond;Glycoprotein;Hydrolase;Lignin degradation;Secreted;Serine esterase;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25425346}. |
Modified Residue | |
Post Translational Modification | PTM: N-glycosylated (PubMed:25425346). {ECO:0000269|PubMed:25425346}. |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (6) |
Cross Reference PDB | 6RTV; 6RU1; 6RU2; 6RV7; 6RV8; 6RV9; |
Mapped Pubmed ID | 32094331; |
Motif | MOTIF 284..289; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
Gene Encoded By | |
Mass | 49,910 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 mM for benzyl (methyl 4-O-methyl-alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=80 mM for benzyl (methyl alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=55 mM for phenylpropyl (methyl alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=8.9 mM for phenyl (methyl alpha-D-glucopyranoside) uronate {ECO:0000269|PubMed:25425346}; KM=4.6 mM for threo-l-[4-(benzyloxy)-3-methoxyphenyl]-3-hydroxy-2- (2-methoxyphenoxy) propyl (methyl 4-O-methyl-alpha-D-glucopyranosid) uronate {ECO:0000269|PubMed:26712478}; |
Metal Binding | |
Rhea ID | RHEA:67452; RHEA:67453 |
Cross Reference Brenda | 3.1.1.B11; |