| IED ID | IndEnz0020000008 |
| Enzyme Type ID | mannase000008 |
| Protein Name |
Beta-mannosidase B EC 3.2.1.25 Mannanase B Mannase B |
| Gene Name | man9 bmann9 mnd2I mndB |
| Organism | Thermothelomyces thermophilus (Myceliophthora thermophila) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Thermothelomyces Thermothelomyces thermophilus (Myceliophthora thermophila) |
| Enzyme Sequence | MAPRVVIPLDQNWEFRQADKPDSKFLPVSQFPTNVHLDLQHHGLIPDPFIGKNELLVQWVGEAQWTYRTVFAAPPVPEGARAVIAFDGLDTFATVVLNGTTILESDNMFLPHRVEVTSVLKAEGNELVITFDSAYLRGCKLVEQHPNHKWGCWNGDVSRLAVRKAQYHWGWDWGPTLLTCGPWRPVHLEIYESRLSDLYAETVVDKSLKRASVKVTAVAERRADRVRFDIALDGQQVATETAELDATSGEATVSFLIDSPALWYPVRYGKQPLYDIRATLLAGDDEVDTLSKRIGLRRAELIQRPLEGQPGTSFFFEVNNIRIYCGGSDWIPADNFIPRISRRRYYDWVRLVAEGNQFMIRVWGGGIYEEQAFYDACDELGILVWQDFMFGCGNYPAWPALLESIRREATENVKRLRHHPSIVIWAGNNEDYQYQESEGLTYDYANKDAESWLKTDFPARYIYEKILADVCADLVPSTPYHPGSPWGAGLNTHDATVGDIHQWNVWHGTQEKWQNFDRLVGRFVSEFGMQAFPAVKTIDAYLPLGRDDPDRYPQSSTVDFHNKAEGHERRIALYLVENLRYAPDPLEHFVYCTQLMQGECLASAYRLWKREWRGPGREYCGGALVWQTNDCWPVTSWSIVDYYLRPKLAYFTVKREMAPVSIGITRRTHLHPRDRHTRVNVDVKTQIEVWASNLTLEDLTVDCVLKAWDVESGEETFSETVAAALLLRENRSTEIAALDVPVRQKNVGEEGRIVVAAYLVDKEGRQMARYVNWPEPLKYVHLQKPRALRAQLTADYSAVEVSAEVPVKGVALECEDDGVRFDDNLVDIVPGEVVTIGVSGAGKDTKIETRYLGMI |
| Enzyme Length | 855 |
| Uniprot Accession Number | I2C092 |
| Absorption | |
| Active Site | ACT_SITE 430; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.; EC=3.2.1.25; |
| DNA Binding | |
| EC Number | 3.2.1.25 |
| Enzyme Function | FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Prefers mannobiose over mannotriose. Is also severely restricted by galactosyl substitutions at the +1 subsite (By similarity). Has no activity against polymeric mannan. {ECO:0000250, ECO:0000269|PubMed:23240568}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:23240568}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.3. Active from pH 4.2 to 6.5. {ECO:0000269|PubMed:23240568}; |
| Pathway | PATHWAY: Glycan metabolism; N-glycan degradation. |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (3) |
| Keywords | Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23240568}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 97,352 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.41 mM for p-nitrophenyl-beta-mannopyranoside {ECO:0000269|PubMed:23240568}; Note=kcat is 15 sec(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |