4S3R

Amylomaltase MalQ from Escherichia coli in complex with the pseudo-heptasaccharide acarviosine-glucose-acarbose

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	malQ	e4s3rA2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: malQ	ECOD (1.6)
A	Glyco_hydro_77	e4s3rA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_77	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF21226	MalQ N-terminal beta sandwich domain (MalQ_N)	MalQ N-terminal beta sandwich domain	Amylomaltase MalQ is essential for the metabolism of maltose and maltodextrins in Escherichia coli. It catalyzes transglycosylation/disproportionation reactions in which glycosyl or dextrinyl units are transferred among linear maltodextrins of variou ...	Amylomaltase MalQ is essential for the metabolism of maltose and maltodextrins in Escherichia coli. It catalyzes transglycosylation/disproportionation reactions in which glycosyl or dextrinyl units are transferred among linear maltodextrins of various lengths [2]. This domain called N2 resembles a beta-sandwich consisting of a five-stranded mixed beta-sheet and a short two-stranded antiparallel beta-sheet. The N2 structure is reminiscent of carbohydrate-binding modules (CBMs) [2]. However, a comparison with structurally known CBMs did not reveal significant similarities.	Domain
A	PF02446	4-alpha-glucanotransferase (Glyco_hydro_77)	4-alpha-glucanotransferase	These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	4-alpha-glucanotransferase	glycosyltransferase activity 4-alpha-glucanotransferase activity transferase activity hexosyltransferase activity catalytic activity	carbohydrate metabolic process catabolic process maltose catabolic process oligosaccharide catabolic process oligosaccharide metabolic process carbohydrate catabolic process primary metabolic process disaccharide metabolic process maltose metabolic process metabolic process cellular process disaccharide catabolic process glucan biosynthetic process polysaccharide biosynthetic process carbohydrate metabolic process catabolic process maltose catabolic process oligosaccharide catabolic process oligosaccharide metabolic process carbohydrate catabolic process primary metabolic process disaccharide metabolic process maltose metabolic process metabolic process cellular process disaccharide catabolic process glucan biosynthetic process polysaccharide biosynthetic process energy derivation by oxidation of organic compounds carbohydrate biosynthetic process glycogen metabolic process generation of precursor metabolites and energy glycogen biosynthetic process macromolecule biosynthetic process polysaccharide metabolic process glucan metabolic process biosynthetic process energy reserve metabolic process macromolecule metabolic process glucan catabolic process macromolecule catabolic process glycogen catabolic process polysaccharide catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR048458	MalQ, N-terminal beta-sandwich domain	Domain
A	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A	IPR003385	Glycoside hydrolase, family 77	Family

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.