Detail Information for IndEnz0008000054
IED ID IndEnz0008000054
Enzyme Type ID cellulase000054
Protein Name 1,4-beta-D-glucan cellobiohydrolase C
EC 3.2.1.91
Beta-glucancellobiohydrolase C
Exocellobiohydrolase C
Exoglucanase C
Gene Name cbhC AN5282
Organism Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Enzyme Sequence MHYSASGLALAFLLPAIQAQQTLYGQCGGSGWTGATSCVAGAACSTLNQWYAQCLPAATTTSTTLTTTTSSVTTTSNPGSTTTTSSVTVTATASGNPFSGYQLYVNPYYSSEVQSIAIPSLTGTLSSLAPAATAAAKVPSFVWLDVAAKVPTMATYLADIRSQNAAGANPPIAGQFVVYDLPDRDCAALASNGEFAISDGGVQHYKDYIDSIREILVEYSDVHVILVIEPDSLANLVTNLNVAKCANAQSAYLECTNYAVTQLNLPNVAMYLDAGHAGWLGWPANLQPAANLYAGVYSDAGSPAALRGLATNVANYNAWAIDTCPSYTQGNSVCDEKDYINALAPLLRAQGFDAHFITDTGRNGKQPTGQQAWGDWCNVIGTGFGARPSTNTGDSLLDAFVWVKPGGESDGTSDTSAARYDAHCGYSDALQPAPEAGTWFQAYFVQLLQNANPSF
Enzyme Length 455
Uniprot Accession Number Q5B2E8
Absorption
Active Site ACT_SITE 185; /evidence=ECO:0000255|PROSITE-ProRule:PRU10056; ACT_SITE 231; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10057; ACT_SITE 410; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10056
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91;
DNA Binding
EC Number 3.2.1.91
Enzyme Function FUNCTION: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. Active against carboxymethylcellulose, beta-glucan and lichenan. {ECO:0000269|PubMed:16844780}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 57 degrees Celsius. {ECO:0000269|PubMed:16844780};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:16844780};
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (4); Domain (1); Erroneous gene model prediction (2); Region (3); Signal peptide (1)
Keywords Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 47,624
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.91;