| Activities in Sub Family | [retaining] α-amylase (EC 3.2.1.1); [retaining] maltogenic α-amylase (EC 3.2.1.133); |
|---|---|
| Mechanism | Retaining a |
| Clan | GH-H |
| 3D Structure Status | ( β / α ) 8 barrel |
| Catalytic Nucleophile/Base | Asp (experimental) |
| Catalytic Proton Donor | Glu (experimental) |
| Note | New: many members have been assigned to subfamilies as described by Stam et al. (2006) Protein Eng Des Sel. 19, 555-562 (PMID: 17085431) |
| External resources | CAZypedia; EBI Protein of the Month; HOMSTRAD; PDB Molecule of the Month; PRINTS; |
| Commercial Enzyme Provider(s) | MEGAZYME; PROZOMIX; |
| Statistics | GenBank accession (899); Uniprot accession (11); PDB accession (4); 3D entries (2); cryst (0) |
| Bacteria | |||||||||||||||
| Protein Name | EC# | Organism | GenBank | Uniprot |
| Subf | |||||||||
| α-amylase (ASKA) | 3.2.1.1 | Anoxybacillus sp. SK3-4 | AFI49455.1 | I1VWH9 |
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45 | |||||||||
| α-amylase (GTA;GTCCBUS3UF5_7870) | 3.2.1.1 | Geobacillus thermoleovorans CCB_US3_UF5 | AEV18110.1 | G8N704 |
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45 | |||||||||
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