Detail Information for IndEnz0010001150
IED ID IndEnz0010001150
Enzyme Type ID esterase001150
Protein Name 4-O-methyl-glucuronoyl methylesterase
EC 3.1.1.117
Glucuronoyl esterase
GCE
GE
Gene Name PHACADRAFT_247750
Organism Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora carnosa)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Phanerochaetaceae Phanerochaete Phanerochaete carnosa Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora carnosa)
Enzyme Sequence MAFRWLSFLLLALPVLALPQTSSKEAQSFGCSTPANIPFNDDKLPDPFLFNDGTPVRSLTDWSCRRQQLASLIQGYEAGTLPPKPPIVTSTFSQNGLTGNLTVTAGFPGNTTTFSSPVTFPNGTVPTEGWPLLIAYSGLSIPIPDGIAVLTYDNSAIGEQNDQTSRGVGQFFDVYGHNATASAMSAWVWGVSRIIDVLEVTPAAHVNTAKIAVTGCSRDGKGALMAGAFEERIALTIPQESGSGGDTCWRLSKFEQDSGDVVQQATEIVQENVWFSTNFDNFVFNISVLPYDHHSLAGLIAPRPMISYENTDFEWLSPLSGFGCMTAAHPIWEAMGVPDNHGFVQVGNHSHCEFPSDLNPTLFAFFDKFLLGKEANTTIFETNEVFNGTVWNPSQWINWTTPTLSH
Enzyme Length 406
Uniprot Accession Number K5XDZ6
Absorption
Active Site ACT_SITE 217; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:G2QJR6; ACT_SITE 351; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:G2QJR6
Activity Regulation
Binding Site BINDING 221; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 263; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 271; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 315; /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:22924998, ECO:0000269|PubMed:24997793};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:22924998, ECO:0000305|PubMed:24997793};
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. {ECO:0000269|PubMed:22924998, ECO:0000269|PubMed:24997793}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:22924998};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:22924998};
Pathway
nucleotide Binding
Features Active site (2); Binding site (4); Chain (1); Disulfide bond (3); Glycosylation (9); 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:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 215..220; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6
Gene Encoded By
Mass 44,170
Kinetics
Metal Binding
Rhea ID RHEA:67452; RHEA:67453
Cross Reference Brenda 3.1.1.B11;