1BYA

CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1byaa_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	Amylase, catalytic domain	beta-Amylase	soybean (Glycine max ) [TaxId: 3847 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	(Trans)glycosidases	8033081	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)
A	PF01373	e1byaA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF01373	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01373	Glycosyl hydrolase family 14 (Glyco_hydro_14)	Glycosyl hydrolase family 14	This family are beta amylases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	BETA-AMYLASE	hydrolase activity, acting on glycosyl bonds amylopectin maltohydrolase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity amylase activity beta-amylase activity	carbohydrate metabolic process catabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process organic substance metabolic process polysaccharide catabolic process metabolic process macromolecule metabolic process organic substance catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001371	Glycoside hydrolase, family 14B, plant	Family
A	IPR001554	Glycoside hydrolase, family 14	Family
A	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A	IPR018238	Glycoside hydrolase, family 14, conserved site	Conserved Site

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	beta-amylase M-CSA #436	Beta-amylase (alpha-1,4-glucan maltohydrolase; EC 3.2.1.2) catalyses the release of beta-anomeric maltose from the non-reducing ends of starch. It is known to function by multiple attack, several maltose molecules being produced before the maltooligosaccharide chain is released from the active site. Although known to bind a calcium ion, the metal is not involved in catalysis. On the basis of its sequence alignment, beta-amylase has been classified as belonging to the glycoside hydrolase family 14 (GH14). It is an inverting glycoside hydrolase that is distributed throughout higher plants, oomycetes and bacteria. However, on the basis of sequence comparisons, plant and bacterial beta-amylases can be readily distinguished from each other.	Defined by 5 residues: ASP:A-101GLU:A-186THR:A-342GLU:A-380LEU:A-383 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.2.1.2 (PDB Primary Data) Search M-CSA Motif + EC 3.2.1.2

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.