Annotations: 6BS6

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	CBM58_SusG	e6bs6A1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: CBM58 (From Topology)	T: CBM58	F: CBM58_SusG	ECOD (1.6)
A	Malt_amylase_C_7	e6bs6A2	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: Malt_amylase_C_7	ECOD (1.6)
A	Alpha-amylase	e6bs6A3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Alpha-amylase	ECOD (1.6)
B	CBM58_SusG	e6bs6B2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: CBM58 (From Topology)	T: CBM58	F: CBM58_SusG	ECOD (1.6)
B	Malt_amylase_C_7	e6bs6B3	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: Malt_amylase_C_7	ECOD (1.6)
B	Alpha-amylase	e6bs6B1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Alpha-amylase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1180	Mainly Beta	Sandwich	Immunoglobulin-like	Golgi alpha-mannosidase II	CATH (4.3.0)
A	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
A	3.90.400.10	Alpha Beta	Alpha-Beta Complex	Oligo-1,6-glucosidase	domain 2	CATH (4.3.0)
A	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
B	2.60.40.1180	Mainly Beta	Sandwich	Immunoglobulin-like	Golgi alpha-mannosidase II	CATH (4.3.0)
B	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
B	3.90.400.10	Alpha Beta	Alpha-Beta Complex	Oligo-1,6-glucosidase	domain 2	CATH (4.3.0)
B	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	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, B	PF20756	Alpha-amylase SusG, CBM58 domain (SusG_CBM58)	Alpha-amylase SusG, CBM58 domain	Enzymes of the Glycoside hydrolase family 13 typically show three domains A, B and C. In addition to these, Alpha-amylase SusG from Bacteroides thetaiotaomicron (Swiss:Q8A1G3) includes the insertion of a unique carbohydrate binding module (CBM) famil ...	Enzymes of the Glycoside hydrolase family 13 typically show three domains A, B and C. In addition to these, Alpha-amylase SusG from Bacteroides thetaiotaomicron (Swiss:Q8A1G3) includes the insertion of a unique carbohydrate binding module (CBM) family 58 (this entry), which gives the protein an elongated shape. SusG, located on the outer membrane of the cell, cleaves starch into oligosaccharides before internalisation for degradation. CBM58 is approximately 120 residues in length. This domain folds into a beta sandwich and adopts an immunoglobulin-like topology with a flat five-stranded antiparallel beta sheet opposing a four-stranded antiparallel beta sheet which features three protruding loops. Y260, W287, and W299 form the starch-binding site [1, 2, 3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Alpha-amylase SusG	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding calcium ion binding starch binding polysaccharide binding carbohydrate binding hydrolase activity, acting on glycosyl bonds amylase activity alpha-amylase activity hydrolase activity, hydrolyzing O-glycosyl compounds cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding calcium ion binding starch binding polysaccharide binding carbohydrate 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 glucan catabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process glucan metabolic process starch metabolic process polysaccharide catabolic process starch catabolic process metabolic process cellular process macromolecule metabolic process carbohydrate metabolic process catabolic process glucan catabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process glucan metabolic process starch metabolic process polysaccharide catabolic process starch catabolic process metabolic process cellular process macromolecule metabolic process oligosaccharide catabolic process oligosaccharide metabolic process	cellular anatomical structure membrane outer membrane cell periphery cell outer membrane external encapsulating structure cell envelope

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR045857	Oligo-1,6-glucosidase, domain 2	Homologous Superfamily
A, B	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A, B	IPR006047	Glycosyl hydrolase, family 13, catalytic domain	Domain
A, B	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A, B	IPR013780	Glycosyl hydrolase, all-beta	Homologous Superfamily
A, B	IPR048755	Alpha-amylase SusG, CBM58 domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.