| IED ID | IndEnz0008000004 |
| Enzyme Type ID | cellulase000004 |
| 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 | NMR spectroscopy (1); X-ray crystallography (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; |