| IED ID | IndEnz0010000175 |
| Enzyme Type ID | esterase000175 |
| Protein Name |
Multidomain esterase Includes: Acetylxylan esterase EC 3.1.1.72 ; 4-O-methyl-glucuronoyl methylesterase EC 3.1.1.117 Glucuronoyl esterase GE |
| Gene Name | cesA |
| Organism | Ruminococcus flavefaciens |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Ruminococcus Ruminococcus flavefaciens |
| Enzyme Sequence | MKKHFVVGETIKRFLRIGTSLALSISTLSLLPSAPRLSSAAGTIKIMPLGDSITYGMADEGGYRKYLSYFLQQKGYTNVDLVGPEGKDSASFNYNGQSVKYDDNHAGYSGYTITNLPGGWFGQLNGILETMQGGDYIKKYSPDIILLQIGTNDVSNGHLDGSEERLHKLLDYLRENMPSNGKVFLTTIPDLGNSGWGGNSNGDIAKYNELIKKVANDYSSKNVIYADIHSVIDASKDLADGVHPNAGGYEKMGKYWLEQIEGYLKASDGPQQTQPTQPSQGDSGPELIYGDLDGDKTITSFDAVIMRKGLINDFKDNNVKKAADIDQNGKAEVADLVQLQSFIIGKIKEFTVAEKTVTEKPVFEKSYNFPAVNQLKSSKDIPDPFIFMDGSKVESTDDWWKRQSEISCMYEYYMYGKWIDGSDDETTYSISGNSMTINVKRKSTGKTASFKAVINLPKNVRHEGGAPVILGMHKGISESTATSNGYAVITYDSDGMFSAPGTAQDNNQHKGAFYDLYPYGRNWDEQTGDLMAWSWGISRILDALYNGAAKELNINPDSSIVTGVSRYGKAASVCGAFDTRIKMCAPSCSGAGGLALYRYSSVGKTYDFSSKGGSSSYTYKENEPLGSLQASGEQGWFNGRFMEFRNAEQFPMDQHMLGALCCDPDRYLFIIGSCESEDWVNAPSVWMAYLGMKHVWDYVGISDHLAINIHKSGHAVIAEDIEKMVQYFDYHVYGIQPKMNLEELQTSVFALPKNKDSFADTFASKWLY |
| Enzyme Length | 768 |
| Uniprot Accession Number | Q9RLB8 |
| Absorption | |
| Active Site | ACT_SITE 68; /note=Nucleophile; for acetylxylan esterase activity; /evidence=ECO:0000250|UniProtKB:Q00017; ACT_SITE 240; /note=For acetylxylan esterase activity; /evidence=ECO:0000250|UniProtKB:Q00017; ACT_SITE 243; /note=For acetylxylan esterase activity; /evidence=ECO:0000250|UniProtKB:Q00017; ACT_SITE 565; /note=Nucleophile; for glucuronoyl esterase activity; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Activity Regulation | |
| Binding Site | BINDING 569; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 633; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 679; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:10846217}; 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:26216754};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:26216754}; |
| DNA Binding | |
| EC Number | 3.1.1.72; 3.1.1.117 |
| Enzyme Function | FUNCTION: Esterase involved in the degradation of plant cell wall polysaccharides. Catalyzes the deacetylation of chemically acetylated xylan and native, steam-extracted xylan (PubMed:10846217). Seems to act in synergy with the xylanase XynD which produces xylo-oligosaccharides (PubMed:10846217). Also catalyzes the deesterification of methyl esters of 4-O-methyl-D-glucuronic acid (MeGlcA) side residues in synthetic glucuronoxylan methyl ester, suggesting that it may be able to cleave ester linkages between MeGlcA carboxyl and more complex alcohols, including linkages between hemicellulose and lignin alcohols in plant cell walls (PubMed:26216754). {ECO:0000269|PubMed:10846217, ECO:0000269|PubMed:26216754}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000305|PubMed:10846217}. |
| nucleotide Binding | |
| Features | Active site (4); Binding site (3); Chain (1); Compositional bias (1); Domain (1); Motif (1); Region (3); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Secreted;Serine esterase;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..40; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 563..568; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Gene Encoded By | |
| Mass | 84,835 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:67452; RHEA:67453 |
| Cross Reference Brenda | 3.1.1.B11; |