| Activities in Family | [retaining] α-amylase (EC 3.2.1.1); |
|---|---|
| Mechanism | Retaining a |
| Clan | GH-T |
| 3D Structure Status | ( β / α ) 7 barrel |
| Catalytic Nucleophile/Base | Glu |
| Catalytic Proton Donor | Asp |
| Note | Distantly related to family GH57; created after Watanabe H, Nishimoto T, Kubota M, Chaen H, Fukuda S. (2006) Biosci Biotechnol Biochem. 2006 Nov;70(11):2690-702 [PMID - 17090949] |
| External resources | CAZypedia; |
| Statistics | GenBank accession (77); Uniprot accession (3); |
| Bacteria | |||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | |
| α-amylase (AgaGH119; LQZ07_19860) | 3.2.1.1 | pubmed |
Agarivorans sp. B2Z047 | UQN42000.1 | |||
| α-amylase (CocoGH19; COCOR_01735) | 3.2.1.1 | pubmed |
Corallococcus coralloides DSM 2259 | AFE08276.1 | H8N1C7 | ||
| α-amylase (FlavoGH119; MKO97_05865) | 3.2.1.1 | pubmed |
Flavobacterium sp. HJ-32-4 | UMY66904.1 | |||
| α-amylase (MasiGH119; DPH57_16015) | 3.2.1.1 | pubmed |
Massilia sp. YMA4 | AXA92520.1 | A0A7U5Y0I1 | ||
| α-amylase (IgtZ) | 3.2.1.1 | pubmed |
Niallia circulans AM7 | BAF37284.1 | A0P8X0 | ||
| α-amylase (ThhaGH119; H3N35_19050) | 3.2.1.1 | pubmed |
Thalassomonas haliotis A5K-61T | WDE10355.1 | |||
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