| Activities in Sub Family | [retaining] α-amylase (EC 3.2.1.1); [retaining] neopullulanase (EC 3.2.1.135); |
|---|---|
| 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 (590); Uniprot accession (0); PDB accession (5); 3D entries (2); cryst (0) |
| Bacteria | ||||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | Subf | |
| α-amylase / neopullulanase (BoSusG; BoGH13A; Bovatus_03803) | 3.2.1.1 3.2.1.135 |
pubmed |
Bacteroides ovatus ATCC 8483 | ALJ48408.1 | 8DGE[A,B,C,D] 8DL1[A,B,C,D] 8DL2[A,B,C,D] |
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