4AYQ

Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with mannoimidazole

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Seven-hairpin glycosidases	8080127	3000996	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	Glyco_hydro_47	e4ayqA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: Glyco_hydro_47	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.50.10.10	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01532	Glycosyl hydrolase family 47 (Glyco_hydro_47)	Glycosyl hydrolase family 47	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding mannosyl-oligosaccharide mannosidase activity hydrolase activity, acting on glycosyl bonds mannosyl-oligosaccharide 1,2-alpha-mannosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds mannosidase activity hydrolase activity alpha-mannosidase activity catalytic activity	cellular response to stimulus catabolic process response to stimulus proteolysis involved in protein catabolic process carbohydrate derivative metabolic process ubiquitin-dependent glycoprotein ERAD pathway macromolecule catabolic process response to glycoprotein ERAD pathway cellular response to stress response to stress proteolysis protein metabolic process protein modification process cellular response to stimulus catabolic process response to stimulus proteolysis involved in protein catabolic process carbohydrate derivative metabolic process ubiquitin-dependent glycoprotein ERAD pathway macromolecule catabolic process response to glycoprotein ERAD pathway cellular response to stress response to stress proteolysis protein metabolic process protein modification process response to endoplasmic reticulum stress mannose trimming involved in glycoprotein ERAD pathway protein alpha-1,2-demannosylation carbohydrate derivative catabolic process glycoprotein catabolic process response to oxygen-containing compound primary metabolic process response to nitrogen compound proteasomal protein catabolic process protein catabolic process glycoprotein metabolic process protein deglycosylation involved in glycoprotein catabolic process response to chemical macromolecule modification protein deglycosylation protein demannosylation metabolic process cellular process macromolecule metabolic process carbohydrate metabolic process	cellular anatomical structure membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR012341	Six-hairpin glycosidase-like superfamily	Homologous Superfamily
A	IPR036026	Seven-hairpin glycosidases	Homologous Superfamily
A	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A	IPR050749	Glycosyl Hydrolase Family 47	Family
A	IPR001382	Glycoside hydrolase family 47	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.