| IED ID | IndEnz0010001135 |
| Enzyme Type ID | esterase001135 |
| Protein Name |
4-O-methyl-glucuronoyl methylesterase EC 3.1.1.117 Glucuronoyl esterase 1 GE1 |
| Gene Name | ge1 Pa_0_910 PODANS_0_910 |
| Organism | Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Podosporaceae Podospora Podospora anserina (Pleurage anserina) Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
| Enzyme Sequence | MVSQTVVSSLLVVLGAAGVRAQQRQSLWGQCGGSGWSGPTLCVDGAWCNPQNQWYHQCIPGSGPTTAQPQVPTTTARPTTTLVTSVVSSTTSPSGPVVTNPPVNPGTCPNTPSGLGTPVANQLNDPFTFHNGNKVTSKADWACRQREISELLQRYELGTLPPKPSSVTASFSGSTLSISVSEGGKSISFTVSINNRPSGAGPHPAIINFGTFGASLPVPAGVATINFNNDDIAQQQGGSSRGRGKFYDLYGSSHSAGALTAWAWGVSRIVDALELTQAQTGIDPTRLGVTGCSRNGKGAIVAGALEPRIALTLPQESGAGGSGCWRIATWQKNNGQNVQDSTQIVQENVWFSPNFNSYVNNVNQLPFDHHLLAGLIAPRALYVMENVDMEWLGKISTYGCMGIARKQWEALGALDNFGYSQVGGNSHCSFPSSQQGSELNAFIEKFLLKRSGGNTNIFRSTQTHSSFNLNNWSPWAVPSLN |
| Enzyme Length | 481 |
| Uniprot Accession Number | B2ABS0 |
| Absorption | |
| Active Site | ACT_SITE 293; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:G2QJR6; ACT_SITE 427; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Activity Regulation | |
| Binding Site | BINDING 297; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 339; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 347; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 391; /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:24531271};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:24531271}; |
| 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:24531271}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Disulfide bond (3); Domain (1); 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:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 291..296; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Gene Encoded By | |
| Mass | 50,942 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.6 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside {ECO:0000269|PubMed:24531271}; KM=2.66 mM for trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate {ECO:0000269|PubMed:24531271}; KM=0.94 mM for 3-phenyl-1-propyl D-glucopyranosyluronate {ECO:0000269|PubMed:24531271}; KM=1.34 mM for 3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate {ECO:0000269|PubMed:24531271}; Note=kcat is 16.2 min(-1) with 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside, 315.3 min(-1) with trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate, 46.5 min(-1) with 3-phenyl-1-propyl D-glucopyranosyluronate and 11.4 min(-1) with 3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate as substrate. {ECO:0000269|PubMed:24531271}; |
| Metal Binding | |
| Rhea ID | RHEA:67452; RHEA:67453 |
| Cross Reference Brenda | 3.1.1.B11; |