Q9P8P3 · GUX1_TRIHA
- ProteinExoglucanase 1
- Genecbh1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids505 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (PubMed:21876370).
The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs 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)
The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs 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)
Catalytic activity
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.4 mM | p-nitrophenyl-D-cellobioside | |||||
3.7 mM | 2-chloro-4-nitrophenyl-beta-lactoside |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.016 mmol/min/mg | for p-nitrophenyl-D-cellobioside | ||||
0.031 mmol/min/mg | for 2-chloro-4-nitrophenyl-beta-lactoside |
kcat is 23.2 min-1 with p-nitrophenyl-D-cellobioside as substrate and 44.6 min-1 with 2-chloro-4-nitrophenyl-beta-lactoside as substrate.
pH Dependence
Optimum pH is 5.0.
Temperature Dependence
Optimum temperature is 50 degrees Celsius.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 225 | Nucleophile | ||||
Sequence: E | ||||||
Active site | 230 | Proton donor/acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | cellulose 1,4-beta-cellobiosidase activity | |
Molecular Function | cellulose binding | |
Biological Process | cellulose catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameExoglucanase 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionQ9P8P3
Subcellular Location
PTM/Processing
Features
Showing features for signal, modified residue, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MYRKLAVISAFLAAARA | ||||||
Modified residue | 18 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000007925 | 18-505 | Exoglucanase 1 | |||
Sequence: QQVCTQQAETHPPLTWQKCTASGCTPQQGSVVLDANWRWTHDTKSTTNCYDGNTWSSTLCPDDATCAKNCCLDGANYSGTYGVTTSGDALTLQFVTASNVGSRLYLMANDSTYQEFTLSGNEFSFDVDVSQLPCGLNGALYFVSMDADGGQSKYPGNAAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGVGGHGSCCSEMDIWEANSISEALTPHPCETVGQTMCSGDSCGGTYSNDRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFALDTTKKLTVVTQFATDGSISRYYVQNGVKFQQPNAQVGSYSGNTINTDYCAAEQTAFGGTSFTDKGGLAQINKAFQGGMVLVMSLWDDYAVNMLWLDSTYPTNATASTPGAKRGSCSTSSGVPAQVEAQSPNSKVIYSNIRFGPIGSTGGNTGSNPPGTSTTRAPPSSTGSSPTATQTHYGQCGGTGWTGPTRCASGYTCQVLNPFYSQCL | ||||||
Disulfide bond | 21↔88 | |||||
Sequence: CTQQAETHPPLTWQKCTASGCTPQQGSVVLDANWRWTHDTKSTTNCYDGNTWSSTLCPDDATCAKNCC | ||||||
Disulfide bond | 36↔41 | |||||
Sequence: CTASGC | ||||||
Disulfide bond | 66↔87 | |||||
Sequence: CYDGNTWSSTLCPDDATCAKNC | ||||||
Disulfide bond | 77↔83 | |||||
Sequence: CPDDATC | ||||||
Glycosylation | 93 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 126 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 151↔410 | |||||
Sequence: CGLNGALYFVSMDADGGQSKYPGNAAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGVGGHGSCCSEMDIWEANSISEALTPHPCETVGQTMCSGDSCGGTYSNDRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFALDTTKKLTVVTQFATDGSISRYYVQNGVKFQQPNAQVGSYSGNTINTDYCAAEQTAFGGTSFTDKGGLAQINKAFQGGMVLVMSLWDDYAVNMLWLDSTYPTNATASTPGAKRGSC | ||||||
Disulfide bond | 185↔223 | |||||
Sequence: CDSQCPRDLKFINGQANVEGWEPSSNNANTGVGGHGSCC | ||||||
Disulfide bond | 189↔222 | |||||
Sequence: CPRDLKFINGQANVEGWEPSSNNANTGVGGHGSC | ||||||
Disulfide bond | 243↔269 | |||||
Sequence: CETVGQTMCSGDSCGGTYSNDRYGGTC | ||||||
Disulfide bond | 251↔256 | |||||
Sequence: CSGDSC | ||||||
Disulfide bond | 274↔344 | |||||
Sequence: CDWNPYRLGNTSFYGPGSSFALDTTKKLTVVTQFATDGSISRYYVQNGVKFQQPNAQVGSYSGNTINTDYC | ||||||
Glycosylation | 283 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 397 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
O-glycosylated. O-glycosylation of the cellulase linker provides protection from proteolysis. Linker glycans also contribute to binding affinity of cellobiohydrolases to cellulose.
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 18-449 | Catalytic | ||||
Sequence: QQVCTQQAETHPPLTWQKCTASGCTPQQGSVVLDANWRWTHDTKSTTNCYDGNTWSSTLCPDDATCAKNCCLDGANYSGTYGVTTSGDALTLQFVTASNVGSRLYLMANDSTYQEFTLSGNEFSFDVDVSQLPCGLNGALYFVSMDADGGQSKYPGNAAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGVGGHGSCCSEMDIWEANSISEALTPHPCETVGQTMCSGDSCGGTYSNDRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFALDTTKKLTVVTQFATDGSISRYYVQNGVKFQQPNAQVGSYSGNTINTDYCAAEQTAFGGTSFTDKGGLAQINKAFQGGMVLVMSLWDDYAVNMLWLDSTYPTNATASTPGAKRGSCSTSSGVPAQVEAQSPNSKVIYSNIRFGPIGSTGGNTGSN | ||||||
Region | 399-423 | Disordered | ||||
Sequence: TASTPGAKRGSCSTSSGVPAQVEAQ | ||||||
Region | 440-472 | Disordered | ||||
Sequence: GSTGGNTGSNPPGTSTTRAPPSSTGSSPTATQT | ||||||
Region | 450-468 | Linker | ||||
Sequence: PPGTSTTRAPPSSTGSSPT | ||||||
Domain | 469-505 | CBM1 | ||||
Sequence: ATQTHYGQCGGTGWTGPTRCASGYTCQVLNPFYSQCL |
Domain
The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.
Sequence similarities
Belongs to the glycosyl hydrolase 7 (cellulase C) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length505
- Mass (Da)53,216
- Last updated2000-10-01 v1
- Checksum52930722F97D7BF0
Keywords
- Technical term