IED ID | IndEnz0010001222 |
Enzyme Type ID | esterase001222 |
Protein Name |
Acetylxylan esterase EC 3.1.1.72 |
Gene Name | axe1 |
Organism | Hypocrea jecorina (Trichoderma reesei) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Hypocrea jecorina (Trichoderma reesei) |
Enzyme Sequence | MPSVKETLTLLLSQAFLATGSPVDGETVVKRQCPAIHVFGARETTVSQGYGSSATVVNLVIQAHPGTTSEAIVYPACGGQASCGGISYANSVVNGTNAAAAAINNFHNSCPDTQLVLVGYSQGAQIFDNALCGGGDPGEGITNTAVPLTAGAVSAVKAAIFMGDPRNIHGLPYNVGTCTTQGFDARPAGFVCPSASKIKSYCDAADPYCCTGNDPNVHQGYGQEYGQQALAFINSQLSSGGSQPPGGGPTSTSRPTSTRTGSSPGPTQTHWGQCGGQGWTGPTQCESGTTCQVISQWYSQCL |
Enzyme Length | 302 |
Uniprot Accession Number | Q99034 |
Absorption | |
Active Site | ACT_SITE 121; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by phenylmethylsulfonyl flouride. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; |
DNA Binding | |
EC Number | 3.1.1.72 |
Enzyme Function | FUNCTION: Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. {ECO:0000269|Ref.2}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (1); Beta strand (7); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (10); Modified residue (1); Propeptide (1); Region (2); Signal peptide (1) |
Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Serine esterase;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | MOD_RES 32; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:9761918 |
Post Translational Modification | PTM: Glycosylated. |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1QOZ; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 30,754 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.1.1.72; |