IED ID | IndEnz0010001148 |
Enzyme Type ID | esterase001148 |
Protein Name |
4-O-methyl-glucuronoyl methylesterase EC 3.1.1.117 Glucuronoyl esterase GE |
Gene Name | Cip2 ce15-1 NCU09445 |
Organism | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Neurospora Neurospora crassa Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
Enzyme Sequence | MVHLTPALLLASAAFAAAAPASQIFERQCSVAGNYPTAAVSKLPDPFTTAAGQKITTKADFDCRKAEISKILQQYELGTYPGKPDKVEGSLSGNTLTVRITVGSQTVSFSASIKKPSSGSGPFPAIIGIGGISIPIPSTVATITFPNDDFAQQSGTSSRGRGKFYTLFGSSHSAGALIAWAWGVDRLVDALEQVQSTSGIDPKRLGVTGCSRNGKGAFVAGALVDRIALTIPQESGAGGAACWRISDSEKSAGKNIQTASQIVTENVWFSPAFNAYTRQTTNIPADHHMLAALTVPRGLIAFENDIDWLGPVSTTACMQAGRLIYKAYGVSNHMGFSLVGGHGHCQFPSSQQSELTSYINYFLLKAGTAPGAVERSSAKVDLKSWAPWDVPALS |
Enzyme Length | 394 |
Uniprot Accession Number | Q7S1X0 |
Absorption | |
Active Site | ACT_SITE 211; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:G2QJR6; ACT_SITE 344; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
Activity Regulation | |
Binding Site | BINDING 215; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 257; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 265; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 308; /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:27600355};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:27600355}; |
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:27600355}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. {ECO:0000269|PubMed:27600355}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. Stable from pH 4 to pH 7. {ECO:0000269|PubMed:27600355}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Binding site (4); Chain (1); Disulfide bond (3); Motif (1); Signal peptide (1) |
Keywords | Disulfide bond;Hydrolase;Lignin degradation;Reference proteome;Secreted;Serine esterase;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G0RV93}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 209..214; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
Gene Encoded By | |
Mass | 41,351 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 mM for 3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate {ECO:0000269|PubMed:27600355}; Note=kcat is 16.8 sec(-1) with 3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate. {ECO:0000269|PubMed:27600355}; |
Metal Binding | |
Rhea ID | RHEA:67452; RHEA:67453 |
Cross Reference Brenda | 3.1.1.B11; |