3.2.1.58: glucan 1,3-beta-glucosidase
This is an abbreviated version!
For detailed information about glucan 1,3-beta-glucosidase, go to the full flat file.
Reaction
+
=
+
Synonyms
1,3-beta-D-glucanohydrolase, AkLam33, ALAM, beta-(1,3)(1,3)-glucanase, beta-(1,3)-glucanase, beta-1,3-exoglucanase, beta-1,3-glucan exo-hydrolase, beta-1,3-glucanase, BGL1, Bglu3B, BGN3.2, BGN3.4, CC1G_06564, CC1G_07313, Celf_3321, ChinLam, Exg, Exg1, EXG2, ExgA, ExgP, exo (13)-beta-glucanase, exo-1,3-beta-D-glucanase, exo-1,3-beta-glucanase, Exo-1,3-beta-glucanase I/II, exo-1,3-beta-glucosidase, Exo-beta 1,3 glucanase, exo-beta-(1,3)-glucanase, exo-beta-(13)-D-glucanase, exo-beta-(13)-glucanohydrolase, exo-beta-1,3-D-glucanase, exo-beta-1,3-glucanase, exo-beta-glucanase, Exo1, Glu1, Glu17A, glucan (1-->3)-beta-glucosidase, GP29, Lam55, Lam55A, lamC, laminarinase, More, panomycocin, PiEXO, tag83, Xog1
ECTree
Posttranslational Modification
Posttranslational Modification on EC 3.2.1.58 - glucan 1,3-beta-glucosidase
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glycoprotein
-
the processed enzyme is N-glycosylated
glycoprotein
the recombinant enzyme is little N-glycosylated
glycoprotein
three potential N-glycosylation sites
glycoprotein
two potential N-glycosylation sites
glycoprotein
Thermochaetoides thermophila
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glycoprotein
Thermochaetoides thermophila DSM 1495
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-
-
proteolytic modification
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the preproprotein is processed sequentially by signal peptidase and a Kex2-like endoprotease to yield a mature protein of 392 amino acids
proteolytic modification
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the preproprotein is processed sequentially by signal peptidase and a Kex2-like endoprotease to yield a mature protein of 392 amino acids
-
proteolytic modification
peroxisome-target-signal at amino acid 11
proteolytic modification
peroxisome-target-signal at amino acid 499
proteolytic modification
signal peptide cleavage site at amino acid 27
proteolytic modification
sequence contains a signal peptide
additional information
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the native enzyme is unglycosylated
additional information
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the native enzyme is unglycosylated
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additional information
the enzyme sequence does not contain a predicted transmembrane domains or a C-terminal glycosylphosphatidylinositol anchor