| IED ID | IndEnz0011000421 |
| Enzyme Type ID | glucanase000421 |
| Protein Name |
Exo beta-1,2-glucooligosaccharide sophorohydrolase non-reducing end EC 3.2.1.214 2-beta-D-glucooligosaccharide sophorohydrolase non-reducing end Beta-1,2-glucanase |
| Gene Name | BDI_3064 |
| Organism | Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Tannerellaceae Parabacteroides Parabacteroides distasonis Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152) |
| Enzyme Sequence | MKHIALLTTLLLSASLQAVEKPYDYVFFENSLMKGDYFYSQAKYTSPSWIKNARHHLPVAGSVAFTPGNSLELTYVSAPGGDWYSEIQYCPVRGNDFFREPSTLSMQVRLRESMNAAALPNIAIRYADSTYTQYLNLRNYLKDTRPGVWHPVSIPLEDFGLNAVNDTNIKKLAAVALRPGTADGNEYTIYLDDIELLPASLPSVSALNAPVLQEAKAYERHIDIKWIPQSKEDIKYYRIYRSFDGITYQPVAVRRPWMNRYTDFLGEVGKKAYYKVTAVDYALNESNDSQTVSATTYPMTDEQLLDMVQEANFRYYWEGAEPNSGLARENIPGRNDMIATGASGFGIMAIVAGIERGFITREEGVQRFLKITSFLEKADKFHGAVSHFIDGTTGKTVAFFGPKDNGGDLVETSFLFQGLLTARQYFNQENDKEKQIRKSIDNLWKNVEWSWYKQFKDSPYLYWHWSPDQAWVINHKLIGWNETMITYMLAIMGPKYGISPEMYYSGWASQEEYAQEYRADWGRVEDGKMYTNGNTYYGENLKVGVSNGGPLFFIHYSYLGLDPHKFTDKYTNYFENNQKMAKINQRYCIENQGGYVGYGEDCWGLTASDFAWNYQAQEPMPHRDNGTMAPTGALASFPYTPDASMKALRNYYRNHGSFLWGEYGFRDAFNLTVNWVSPLFMGLNQAPVTVMIENYRTNLLWNLFMSHPDVQKGIQKIQSIK |
| Enzyme Length | 721 |
| Uniprot Accession Number | A6LGF6 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[(1->2)-beta-D-glucosyl](n) + H2O = [(1->2)-beta-D-glucosyl](n-2) + sophorose; Xref=Rhea:RHEA:62388, Rhea:RHEA-COMP:11881, Rhea:RHEA-COMP:16082, ChEBI:CHEBI:1230, ChEBI:CHEBI:15377, ChEBI:CHEBI:27517; EC=3.2.1.214; Evidence={ECO:0000269|PubMed:29763309}; |
| DNA Binding | |
| EC Number | 3.2.1.214 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of linear beta-1,2-glucan and beta-1,2-glucooligosaccharides with degrees of polymerization (DPs) greater than or equal to 4, to produce sophorose. The best substrates are tetra- and pentasaccharides. Acts as an exo-type enzyme that releases sophorose from the non-reducing end of the substrate. It cannot hydrolyze cyclic beta-1,2-glucans. {ECO:0000269|PubMed:29763309}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:29763309}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:29763309}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (31); Chain (1); Domain (1); Helix (24); Signal peptide (1); Turn (11) |
| Keywords | 3D-structure;Glycosidase;Hydrolase;Periplasm;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:29763309}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5Z06; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 82,568 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 mM for beta-1,2-glucotetrasaccharide {ECO:0000269|PubMed:29763309}; KM=1.6 mM for beta-1,2-glucopentasaccharide {ECO:0000269|PubMed:29763309}; KM=1.0 mM for beta-1,2-glucan (with an average DP of 77) {ECO:0000269|PubMed:29763309}; Note=kcat is 54 sec(-1) with beta-1,2-glucotetrasaccharide as substrate. kcat is 29 sec(-1) with beta-1,2-glucopentasaccharide as substrate. kcat is 0.48 sec(-1) with beta-1,2-glucan (with an average DP of 77) as substrate. {ECO:0000269|PubMed:29763309}; |
| Metal Binding | |
| Rhea ID | RHEA:62388 |
| Cross Reference Brenda | 3.2.1.214; |