Detail Information for IndEnz0005001390
IED ID IndEnz0005001390
Enzyme Type ID lipase001390
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;