| Activities in Sub Family | α-glucosidase (EC 3.2.1.20); Exo-α-1,3-glucanase / α-1,3-glucosidase (EC 3.2.1.84); |
|---|---|
| Mechanism | Retaining a |
| Clan | GH-D |
| 3D Structure Status | ( β / α ) 8 barrel |
| Catalytic Nucleophile/Base | Asp |
| Catalytic Proton Donor | Asp |
| Note | Subfamily classification initiated by Arumapperuma et al. 2023 [PMID:36806678] |
| External resources | CAZypedia; PROSITE; |
| Commercial Enzyme Provider(s) | MEGAZYME; |
| Statistics | GenBank accession (243); Uniprot accession (1); PDB accession (8); 3D entries (1); cryst (0) |
| Bacteria | ||||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | Subf | |
| α-glucosidase (Bl_Glc31; BL1334) | 3.2.1.20 | pubmed |
Bifidobacterium longum NCC2705 | AAN25134.1 NP_696498.1 |
15 | |||
| α-glucosidase with preference for α-1,3-glucosidic bonds (LlGH31_u1; lmg_1836) | 3.2.1.20 3.2.1.84 |
pubmed pubmed |
Lactococcus cremoris subsp. cremoris MG1363 | CAL98407.1 | A2RM80 | 7WJ9[A,B,C,D,E,F] 7WJA[A] 7WJB[A] 7WJC[A] 7WJD[A] 7WJE[A] 7WJF[A] 7WLG[A,B,C,D,E,F] |
15 | |
| Eukaryota | ||||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | Subf | |
| α-glucosidase with preference for α-1,3-glucosidic bonds (Cmgh31) | 3.2.1.20 3.2.1.84 |
pubmed pubmed |
Cordyceps militaris NBRC 103752 | BDC78265.1 | 15 | |||
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