Detail Information for IndEnz0010001139
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;