| Activities in Sub Family | [retaining] α-amylase (EC 3.2.1.1); |
|---|---|
| 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 (325); Uniprot accession (5); |
| Bacteria | ||||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | Subf | |
| multidomain α-amylase (EUR_21100) (cell-wall anchored) | 3.2.1.1 | Agathobacter rectalis DSM 17629 | CBK91127.1 | D6DYI9 | 41 | |||
| alkaline amylase-pullulanase | 3.2.1.1 | pubmed |
Bacillus sp. (in: firmicutes) KSM-1378 | AAS36537.1 AAS36538.1 BAA11332.1 |
P70983 | 41 | ||
| α-amylase | 3.2.1.1 | pubmed |
Micrococcus sp. 207 | CAA39321.1 | Q06812 | 41 | ||
| α-amylase (AmyB) (Amy13A) | 3.2.1.1 | Roseburia sp. A2-194 | CAJ20070.1 | Q3LB10 | 41 | |||
| bifunctional amylopullulanase (ApuA;SSU1849) | 3.2.1.1 | pubmed |
Streptococcus suis P1/7 | CAR47543.1 | C5VVZ9 | 41 | ||
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