UniProt functional annotation for Q99036

UniProt code: Q99036.

Organism: Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei).
Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
 
Function: Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and ivory nut mannan, releasing mainly tri- and disaccharides (PubMed:7793911, Ref.3, Ref.4, PubMed:8529653). Also has transglycosylation activity. Transglycosylation of two mannotrioses into a mannohexaose is the major transglycosylation route (PubMed:8529653, Ref.7, PubMed:24950755). {ECO:0000269|PubMed:24950755, ECO:0000269|PubMed:7793911, ECO:0000269|PubMed:8529653, ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.7}.
 
Catalytic activity: Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.; EC=3.2.1.78; Evidence={ECO:0000269|PubMed:8529653, ECO:0000269|Ref.3, ECO:0000269|Ref.4};
Biophysicochemical properties: Kinetic parameters: KM=0.0015 mg/ml for locust bean gum mannan {ECO:0000269|Ref.3}; KM=0.6 mg/ml for locust bean gum mannan {ECO:0000269|Ref.7}; KM=0.25 mM for 4-methylumbelliferyl-mannotrioside {ECO:0000269|Ref.7}; KM=0.31 mM for mannotetraose {ECO:0000269|Ref.7}; KM=0.08 mM for mannopentaose {ECO:0000269|Ref.7}; KM=0.05 mM for mannohexaose {ECO:0000269|Ref.7}; pH dependence: Optimum pH is 5.0. Stable from pH 2.5 to 7.0. {ECO:0000269|Ref.3}; Temperature dependence: Optimum temperature is 75 degrees Celsius. {ECO:0000269|Ref.3};
Subunit: Monomer. {ECO:0000250|UniProtKB:B2B3C0}.
Subcellular location: Secreted {ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
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 (Probable). The CBM binds to cellulose but not to mannan, and increases the mannan- hydrolysis of complex substrates (PubMed:12523968). {ECO:0000269|PubMed:12523968, ECO:0000305|PubMed:7793911}.
Similarity: Belongs to the glycosyl hydrolase 5 (cellulase A) family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.