Detail Information for IndEnz0008000432
IED ID IndEnz0008000432
Enzyme Type ID cellulase000432
Protein Name Endo-1,4-beta-xylanase 3
Xylanase 3
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase 3
Gene Name xyn3 TRIREDRAFT_120229
Organism Hypocrea jecorina (strain QM6a) (Trichoderma reesei)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Hypocrea jecorina (Trichoderma reesei) Hypocrea jecorina (strain QM6a) (Trichoderma reesei)
Enzyme Sequence MKANVILCLLAPLVAALPTETIHLDPELAALRANLTERTADLWDRQASQSIDQLIKRKGKLYFGTATDRGLLQREKNAAIIQADLGQVTPENSMKWQSLENNQGQLNWGDADYLVNFAQQNGKSIRGHTLIWHSQLPAWVNNINNADTLRQVIRTHVSTVVGRYKGKIRAWDVVNEIFNEDGTLRSSVFSRLLGEEFVSIAFRAARDADPSARLYINDYNLDRANYGKVNGLKTYVSKWISQGVPIDGIGSQSHLSGGGGSGTLGALQQLATVPVTELAITELDIQGAPTTDYTQVVQACLSVSKCVGITVWGISDKDSWRASTNPLLFDANFNPKPAYNSIVGILQ
Enzyme Length 347
Uniprot Accession Number G0RA32
Absorption
Active Site ACT_SITE 176; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01096; ACT_SITE 282; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01096
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000250|UniProtKB:Q9P973};
DNA Binding
EC Number 3.2.1.8
Enzyme Function FUNCTION: Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose. Produces xylobiose and xylotriose as the main degradation products. {ECO:0000250|UniProtKB:Q9P973}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01096}.
nucleotide Binding
Features Active site (2); Beta strand (10); Chain (1); Disulfide bond (1); Domain (1); Helix (16); Modified residue (1); Propeptide (1); Signal peptide (1); Turn (1)
Keywords 3D-structure;Carbohydrate metabolism;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9P973}.
Modified Residue MOD_RES 46; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:Q9P973
Post Translational Modification PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q9P973}.
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000255
Structure 3D X-ray crystallography (1)
Cross Reference PDB 4XV0;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 38,076
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda