Detail Information for IndEnz0011000106
IED ID IndEnz0011000106
Enzyme Type ID glucanase000106
Protein Name Endoglucanase EG-1
EC 3.2.1.4
Cellulase
Endo-1,4-beta-glucanase
Gene Name egl1
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 MAPSVTLPLTTAILAIARLVAAQQPGTSTPEVHPKLTTYKCTKSGGCVAQDTSVVLDWNYRWMHDANYNSCTVNGGVNTTLCPDEATCGKNCFIEGVDYAASGVTTSGSSLTMNQYMPSSSGGYSSVSPRLYLLDSDGEYVMLKLNGQELSFDVDLSALPCGENGSLYLSQMDENGGANQYNTAGANYGSGYCDAQCPVQTWRNGTLNTSHQGFCCNEMDILEGNSRANALTPHSCTATACDSAGCGFNPYGSGYKSYYGPGDTVDTSKTFTIITQFNTDNGSPSGNLVSITRKYQQNGVDIPSAQPGGDTISSCPSASAYGGLATMGKALSSGMVLVFSIWNDNSQYMNWLDSGNAGPCSSTEGNPSNILANNPNTHVVFSNIRWGDIGSTTNSTAPPPPPASSTTFSTTRRSSTTSSSPSCTQTHWGQCGGIGYSGCKTCTSGTTCQYSNDYYSQCL
Enzyme Length 459
Uniprot Accession Number P07981
Absorption
Active Site ACT_SITE 218; /note=Nucleophile; /evidence=ECO:0000269|PubMed:9325098; ACT_SITE 223; /note=Proton donor/acceptor; /evidence=ECO:0000269|PubMed:9325098
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|Ref.2};
DNA Binding
EC Number 3.2.1.4
Enzyme Function FUNCTION: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose (PubMed:2948877). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates new chain ends for exocellobiohydrolases (CBHs). The CBH release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable). {ECO:0000269|PubMed:2948877, ECO:0000305}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (2); Chain (1); Compositional bias (1); Disulfide bond (11); Domain (1); Glycosylation (3); Modified residue (1); Region (3); Signal peptide (1); Site (3)
Keywords 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}.
Modified Residue MOD_RES 23; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:9325098, ECO:0000269|Ref.3"
Post Translational Modification PTM: Asn-204 contains mainly a high-mannose-type glycan (Hex(7-9)GlcNAc(2)), with a small fraction (8%) bearing a single GlcNAc at this site. {ECO:0000250|UniProtKB:A0A024SNB7}.
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000269|Ref.3
Structure 3D X-ray crystallography (1); NMR spectroscopy (1)
Cross Reference PDB 1EG1; 4BMF;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 48,208
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.4;