| Activities in Family | Endo-β-1,3-glucanase / laminarinase (EC 3.2.1.39); |
|---|---|
| Mechanism | Retaining e |
| Clan | GH-A |
| 3D Structure Status | ( β / α ) 8 barrel |
| Catalytic Nucleophile/Base | Glu (experimental) |
| Catalytic Proton Donor | Glu (experimental) |
| Note | The endo-b-1,3-glucanase activity of the Victivallis vadensis enzyme was shown in Helbert et al., PNAS (2019) [PMID=30850540]. The retaining mechanism and catalytic amino acids have been confirmed in Brumer et al., mBio (2020) [PMID:32265336]. |
| External resources | CAZypedia; |
| Statistics | GenBank accession (918); Uniprot accession (2); PDB accession (1); 3D entries (1); cryst (0) |
| Bacteria | |||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | |
| endo-β-1,3-glucanase (BfGH158; HMPREF9446_00612) | 3.2.1.39 | pubmed |
Bacteroides fluxus YIT 12057 | EGF59242.1 | F3PPH2 | ||
| endo-β-1,3-glucanase (BuGH158; BACUNI_01485) | 3.2.1.39 | pubmed |
Bacteroides uniformis ATCC 8492 | ZP_02070068.1 | A0A412SRH5 | 6PAL[A,B] | |
| endo-β-1,3-glucanase active on curdlan (Vvad_PD1638) | 3.2.1.39 | pubmed |
Victivallis vadensis ATCC BAA-548 | ZP_06243608.1 | |||
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