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 (27); Uniprot accession (27); PDB accession (3); 3D entries (2); cryst (0)

Bacteria
Protein Name	EC#	Organism	GenBank	Uniprot	PDB/3D Carbohydrate Ligands Resolution (Å)	Subf
α-amylase (Kra2;PKA)	3.2.1.1	Bacillus sp. KR8104	ACD93218.3 ACD93218.2	B3GQD0	3DC0[A] 2.78	28
α-amylase	3.2.1.1	Bacillus subtilis 2633	CAA30643.1	Q45520	1BAG[A] α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-α-D-Glcp-(1-4)-β-D-Glcp 2.50 1UA7[A] <non_carb>-(1-4)-α-D-6-deoxy-Glcp4N-(1-4)-α-D-Glcp-(1-4)-<non_carb>-(0-4)-α-D-6-deoxy-Glcp4N-(1-4)-β-D-Glcp 2.21	28
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