| IED ID | IndEnz0010001113 |
| Enzyme Type ID | esterase001113 |
| Protein Name |
Carbohydrate acetyl esterase/feruloyl esterase Includes: Carbohydrate acetyl esterase EC 3.1.1.- ; Feruloyl esterase EC 3.1.1.73 Ferulic acid esterase |
| Gene Name | axe1-6A PRU_2707 |
| Organism | Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Prevotellaceae Prevotella Prevotella ruminicola (Bacteroides ruminicola) Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) |
| Enzyme Sequence | MYQSTLKTILLASALLILPASMSAQKRKAAPKKAATEQVGKPDPNFYIFLCFGQSNMEGNARPEAQDLTSPGPRFLLMPAVDFPEKGRKMGEWCEASAPLCRPNTGLTPADWFGRTLVASLPENIKIGVIHVAIGGIDIKGFLPDSIQNYLKVAPNWMKGMLAAYDNNPYERLVTLAKKAQKDGVIKGILMHQGETNTGDPKWAGMVKQVYDNLCGDLNLKPEEVNLYAGNIVQADGKGVCIGCKKQIDELPLTLHTSQVISSDGCTNGPDRLHFDAAGYRELGCRYGEAVARHLGYEPKRPYIEMPKQIEVPADAFIAETTVPGNEFPKVDKEGRAYFRIAAPEARKVVLDICNKKYDMQRDGKGNFMAVTDPLPVGFHYYFLNINGVNFIDPSTETFFGCNRESGGIEIPEGSEGDYYRPQQGVPAGQVRSIYYYSNEQQTWRHAMVYTPAEYELAKNAKKRYPVLYLQHGMGEDETGWSKQGHMQHIMDNAIAKGEAVPMIVVMESGDIKAPFGGGNNQAGRSAYGASFYPVLLNDLIPYIDSNYRTKSDRENRAMAGLSWGGHQTFDVVLTNLDKFAWLGTFSGAIFGLDVKTAYDGVFANADEFNKKIHYMYMNWGEEDFIKSGDIVKQLRELGIKVDSNESKGTAHEWLTWRRGLNEFIPHLFKK |
| Enzyme Length | 671 |
| Uniprot Accession Number | D5EXZ4 |
| Absorption | |
| Active Site | ACT_SITE 55; /note=For acetyl esterase activity; /evidence=ECO:0000250; ACT_SITE 271; /note=For acetyl esterase activity; /evidence=ECO:0000250; ACT_SITE 274; /note=For acetyl esterase activity; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000269|PubMed:21742923}; |
| DNA Binding | |
| EC Number | 3.1.1.-; 3.1.1.73 |
| Enzyme Function | FUNCTION: Involved in degradation of plant cell wall polysaccharides. Bifunctional esterase that possesses both acetyl esterase and ferulic acid esterase activities. Has deacetylase activity towards acetylated xylo-oligosaccharides smaller than xylo-heptaose, as well as from glucose-pentaacetate. Is also able to release ferulic acid from methylferulate, and from the more natural substrates wheat bran, corn fiber, and XOS(FA,Ac), a corn fiber-derived substrate enriched in O-acetyl and ferulic acid esters. {ECO:0000269|PubMed:21742923}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius with glucose-pentaacetate as substrate. Active from 20 to 50 degrees Celsius. Still exhibits 40 to 70% of the maximum activity after 20 hours of incubation at 50 degrees Celsius. {ECO:0000269|PubMed:21742923}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with glucose-pentaacetate as substrate. Active from pH 5.0 to 8.0. {ECO:0000269|PubMed:21742923}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:21742923}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Region (2); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Reference proteome;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: By growth on ester-enriched corn oligosaccharides. {ECO:0000269|PubMed:21742923}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 74,683 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |