Detail Information for IndEnz0010001144
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;