6YQ9

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B [auth BBB]	DUF1966	e6yq9BBB1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: DUF1966	ECOD (1.6)
B [auth BBB]	Alpha-amylase	e6yq9BBB2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Alpha-amylase	ECOD (1.6)
A [auth AAA]	DUF1966	e6yq9AAA2	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: DUF1966	ECOD (1.6)
A [auth AAA]	Alpha-amylase	e6yq9AAA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Alpha-amylase	ECOD (1.6)

Chains	Accession	Name	Description	Comments	Source
A [auth AAA], B [auth BBB]	PF00128	Alpha amylase, catalytic domain (Alpha-amylase)	Alpha amylase, catalytic domain	Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, a ...	Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.	Domain
A [auth AAA], B [auth BBB]	PF09260	Alpha-amylase, domain C (A_amylase_dom_C)	Alpha-amylase, domain C	This domain is found at the C-terminal of various fungal alpha-amylase proteins [1]. It has been identified as a secondary binding site, which might be part of a starch interaction site [2]. It has a beta- sandwich fold comprising an antiparallel bet ...	This domain is found at the C-terminal of various fungal alpha-amylase proteins [1]. It has been identified as a secondary binding site, which might be part of a starch interaction site [2]. It has a beta- sandwich fold comprising an antiparallel beta-sheet with eight strands [2,3].	Domain

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth AAA], B [auth BBB]	Alpha-amylase	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding hydrolase activity, acting on glycosyl bonds amylase activity alpha-amylase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	carbohydrate metabolic process catabolic process carbohydrate catabolic process primary metabolic process metabolic process cellular process	-

Chains	Accession	Name	Type
A [auth AAA], B [auth BBB]	IPR013777	Alpha-amylase-like	Family
A [auth AAA], B [auth BBB]	IPR015340	Alpha-amylase, domain C	Domain
A [auth AAA], B [auth BBB]	IPR006047	Glycosyl hydrolase, family 13, catalytic domain	Domain
A [auth AAA], B [auth BBB]	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A [auth AAA], B [auth BBB]	IPR006046	Alpha amylase	Family
A [auth AAA], B [auth BBB]	IPR013780	Glycosyl hydrolase, all-beta	Homologous Superfamily