ProGP74 (H(A107-M) (1,3-1,4)-beta-glucanase)

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ProGP ID ProGP74 (H(A107-M) (1,3-1,4)-beta-glucanase)
Validation Status Uncharacterized
Organism Information
Organism NamePaenibacillus (Bacillus) amyloliquefaciens (velezensis) and Bacillus macerans
Domain Bacteria
Classification Phylum : Firmicutes
Class : Bacilli
Orders : Bacillales
Family : Bacillaceae
Genus : Paenibacillus
Species : amyloliquefaciens
Taxonomic ID (NCBI) 1390
Genome Information
GenBank M15674
EMBL M15674
Gene Information
Gene NamebglA
Protein Information
Protein NameH(A107-M) (1,3-1,4)-beta-glucanase
UniProtKB/SwissProt ID P07980
Sequence length 239 AA
Subcellular LocationSecreted
Function Catalyses cleavage of (1,4)-beta-linkages of O-substituted beta-D-glucanopyranosyl residues.
Glycosylation Status
Technique(s) used for Glycosylation DetectionCarbohydrate content determination with GLC
Glycan Information
Glycan Annotation The relative molar content of monosaccharides: N-acetylglucosamine 1.0, mannose 4.9, galactose 2.1, glucose 5.5. The relative content of mannose and N-acetylglucosamine indicates the presence of oligomannose or hybrid-type oligosaccharides and the presence of galactose possibly indicates either O-linked or hybrid-types oligosaccharides. Addition of an N-linked oligosaccharide corresponding to an increase in apparent molecular mass of 3 kDa.
Protein Glycosylation linked (PGL) gene(s)
Additional CommentEngineered glycoprotein.
The glucanases from which the hybrid enzyme is made, are not glycosylated in their native hosts. So the hybrid enzyme (214 AA) containing 107 amino acids from Bacillus amyloliquefaciens (1,3-1,4)-beta-glucanase (AMY), and 107 residues from B. macerans (1,3-1,4)-beta-glucanase (MAC), is glycosylated in Saccharomyces cerevisiae to observe its effect on the thermostability of the enzyme. Signal peptide is from MAC.
UniProtKB ID of MAC is P23904 and that of AMY is P07980. UniProtKB and EMBL information has been included for AMY.
Year of Identification1991
Year of Identification Month Wise1991.01
ReferenceMeldgaard, M., 1994. Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1, 3-1, 4)-β-glucanases secreted from yeast. Microbiology, 140(1), pp.159-166.
Corresponding Author Morten Meldgaard
ContactDepartment of Physiology, Carlsberg Laboratory, Copenhagen, Denmark.
ReferenceOlsen, O. and Thomsen, K.K., 1991. Improvement of bacterial β-glucanase thermostability by glycosylation. Microbiology, 137(3), pp.579-585.
Corresponding Author Karl KristianThomesen
ContactCarlsberg Laboratory, Department of Physiology, Gamle Carlsbergvej 10, DK-2500 Copenhagen Valby, Denmark