Detail Information for IndEnz0020000009
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