5BRQ

Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d5brqb2	All beta proteins	Glycosyl hydrolase domain	Glycosyl hydrolase domain	automated matches	automated matches	(Bacillus licheniformis DSM 13 = ATCC 14580 ) [TaxId: 279010 ],	SCOPe (2.08)
B	d5brqb1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	automated matches	automated matches	(Bacillus licheniformis DSM 13 = ATCC 14580 ) [TaxId: 279010 ],	SCOPe (2.08)
C	d5brqc2	All beta proteins	Glycosyl hydrolase domain	Glycosyl hydrolase domain	automated matches	automated matches	(Bacillus licheniformis DSM 13 = ATCC 14580 ) [TaxId: 279010 ],	SCOPe (2.08)
C	d5brqc1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	automated matches	automated matches	(Bacillus licheniformis DSM 13 = ATCC 14580 ) [TaxId: 279010 ],	SCOPe (2.08)
D	d5brqd2	All beta proteins	Glycosyl hydrolase domain	Glycosyl hydrolase domain	automated matches	automated matches	(Bacillus licheniformis DSM 13 = ATCC 14580 ) [TaxId: 279010 ],	SCOPe (2.08)
D	d5brqd1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	automated matches	automated matches	(Bacillus licheniformis DSM 13 = ATCC 14580 ) [TaxId: 279010 ],	SCOPe (2.08)
A	d5brqa2	All beta proteins	Glycosyl hydrolase domain	Glycosyl hydrolase domain	automated matches	automated matches	(Bacillus licheniformis DSM 13 = ATCC 14580 ) [TaxId: 279010 ],	SCOPe (2.08)
A	d5brqa1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	automated matches	automated matches	(Bacillus licheniformis DSM 13 = ATCC 14580 ) [TaxId: 279010 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	(Trans)glycosidases	8099772	3000313	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Glycosyl hydrolase domain-like	8101028	3001528	SCOP2B (2022-06-29)
C	SCOP2 Family	Amylase, catalytic domain	8099771	4003138	SCOP2 (2022-06-29)
C	SCOP2 Family	alpha-Amylases, C-terminal beta-sheet domain	8101027	4002636	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	(Trans)glycosidases	8099772	3000313	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Glycosyl hydrolase domain-like	8101028	3001528	SCOP2 (2022-06-29)
D	SCOP2B Superfamily	Glycosyl hydrolase domain-like	8101028	3001528	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	(Trans)glycosidases	8099772	3000313	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Glycosyl hydrolase domain-like	8101028	3001528	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	(Trans)glycosidases	8099772	3000313	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Malt_amylase_C_2	e5brqB1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: Malt_amylase_C_2	ECOD (1.6)
B	Alpha-amylase	e5brqB2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Alpha-amylase	ECOD (1.6)
C	Malt_amylase_C_2	e5brqC2	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: Malt_amylase_C_2	ECOD (1.6)
C	Alpha-amylase	e5brqC1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Alpha-amylase	ECOD (1.6)
D	Malt_amylase_C_2	e5brqD1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: Malt_amylase_C_2	ECOD (1.6)
D	Alpha-amylase	e5brqD2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Alpha-amylase	ECOD (1.6)
A	Malt_amylase_C_2	e5brqA1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: Malt_amylase_C_2	ECOD (1.6)
A	Alpha-amylase	e5brqA2	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)
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	2.60.40.1180	Mainly Beta	Sandwich	Immunoglobulin-like	Golgi alpha-mannosidase II	CATH (4.3.0)
C	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
C	3.90.400.10	Alpha Beta	Alpha-Beta Complex	Oligo-1,6-glucosidase	domain 2	CATH (4.3.0)
C	2.60.40.1180	Mainly Beta	Sandwich	Immunoglobulin-like	Golgi alpha-mannosidase II	CATH (4.3.0)
D	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
D	3.90.400.10	Alpha Beta	Alpha-Beta Complex	Oligo-1,6-glucosidase	domain 2	CATH (4.3.0)
D	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	2.60.40.1180	Mainly Beta	Sandwich	Immunoglobulin-like	Golgi alpha-mannosidase II	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	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, C, D	PF16657	Maltogenic Amylase, C-terminal domain (Malt_amylase_C)	Maltogenic Amylase, C-terminal domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Glycoside Hydrolase Family 13	hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity trehalase activity alpha,alpha-phosphotrehalase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	carbohydrate metabolic process trehalose catabolic process catabolic process trehalose metabolic process oligosaccharide catabolic process oligosaccharide metabolic process carbohydrate catabolic process primary metabolic process disaccharide metabolic process metabolic process cellular process disaccharide catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR006047	Glycosyl hydrolase, family 13, catalytic domain	Domain
A, B, C, D	IPR045857	Oligo-1,6-glucosidase, domain 2	Homologous Superfamily
A, B, C, D	IPR032091	Maltogenic amylase-like, C-terminal	Domain
A, B, C, D	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A, B, C, D	IPR012769	Trehalose-6-phosphate hydrolase	Family
A, B, C, D	IPR013780	Glycosyl hydrolase, all-beta	Homologous Superfamily

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.