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; |