IED ID | IndEnz0020000009 |
Enzyme Type ID | mannase000009 |
Protein Name |
Beta-mannosidase B EC 3.2.1.25 Mannanase B Mannase B |
Gene Name | mndB AN3368 |
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 | MGAFTQHVLSEGWSFKDSGDQSPDAWLSVPTVPSVVHQDLQANGKLDDPFIGLNELSARWVNEKSWTYRNVFQKPTVPAGSSIFLVFDGLDTFAKVKLDGQVILESDNMFLAHRVDITKALDVEGEHTLEIDFDCALLRARELRKQHPDHKWVGFNGDTARLSVRKAQYHWGWDWGPVLMTAGIWKEVRLEVYSAKISDLWTEVHLAEDHSKARITAAAEVETQGTGNSYKATFTLSLQGQQIGKEVATLDGNVAKTTFDVQEPSLWWPNGYGDQTLYEISVSLEKEEEQAHQVSKKFGIRTAEVIQRPDKHGKSFFFRINGVDIFCGGACWIPADSLLTNITPDRYRKWIELMAVGHQVMIRVWGGGIYEDESFYQACDEVGVMVWQDFMFGCGNYPTWPEILESIEKEAEYNLRRLRHHPSIVIWVGNNEDYQVQEQQGLTYNYADKDPESWLKTDFPARYIYEHLLPKAVQKIIPSAYYHPGSPWGDGKITSDPTVGDMHQWNVWHGTQEKYQIFDTLGGRFNSEFGMEAFPHMSTIDHFVTNEADKYPQSHVLDFHNKADGHERRIATYLVENLRTATDLEVYIYLTQVVQAETMMFGYRGWRRQWGDERHCGGALLWQLNDCWPTISWAIVDYFLRPKPAFYAVSRVLKPLAIGVRREHHDWSVSHAQPPKTSKYELWVVSSLLKEVIGKVELRFISIKTGLAIHESIVRENVTIVPNGTTNILDGVIDHAVDEPHVLAARLWVDGELVARDVDWPQPFKYLDLSDRGLEITRISKTESEQVLELSARKPVKCLVFEERDNVRVSDSAIDIVPGDEQFVTIKGLKRSDAPLKYKFLGQ |
Enzyme Length | 843 |
Uniprot Accession Number | Q5B7W2 |
Absorption | |
Active Site | ACT_SITE 432; /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 and has no activity against polymeric mannan. Is also severely restricted by galactosyl substitutions at the +1 subsite. Releases the terminal mannose residue from mannobiose, mannotriose and galactosyl-mannotriose (GM3), but not from galactosyl-mannobiose (GM2) or di-galactosyl-mannopentaose (G2M5). {ECO:0000269|PubMed:16844780, ECO:0000269|PubMed:24021641}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius (at pH 6). {ECO:0000269|PubMed:24021641}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Active from pH 5 to 8. {ECO:0000269|PubMed:24021641}; |
Pathway | PATHWAY: Glycan metabolism; N-glycan degradation. |
nucleotide Binding | |
Features | Active site (1); Chain (1); Erroneous gene model prediction (2) |
Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 96,367 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 mM for p-nitrophenyl-beta-mannopyranoside {ECO:0000269|PubMed:24021641}; Note=kcat is 79.2 min(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |