Annotations: 5JOU

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	YicI C-terminal domain-like	8090401	3000267	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Glycosyl hydrolase domain-like	8090405	3001528	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Galactose mutarotase-like	8090400	3000035	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	(Trans)glycosidases	8090403	3000313	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	galactose-binding domain-like	8090407	3000087	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Galactose mutarotase-like	8090400	3000035	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_31_C	e5jouA5	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: Glyco_hydro_31_C	ECOD (1.6)
A	Gal_mutarotas_2	e5jouA3	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Gal_mutarotas_2	ECOD (1.6)
A	DUF5110	e5jouA2	A: beta sandwiches	X: Putative glucosidase YicI, C-terminal domain (From Topology)	H: Putative glucosidase YicI, C-terminal domain (From Topology)	T: Putative glucosidase YicI, C-terminal domain	F: DUF5110	ECOD (1.6)
A	PA14	e5jouA1	A: beta sandwiches	X: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	H: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	T: N-terminal beta-sandwich domain in anthrax protective antigen	F: PA14	ECOD (1.6)
A	Glyco_hydro_31_N	e5jouA4	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_31_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1760	Mainly Beta	Sandwich	Immunoglobulin-like	glycosyl hydrolase (family 31)	CATH (4.3.0)
A	2.60.120.380	Mainly Beta	Sandwich	Jelly Rolls		CATH (4.3.0)
A	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	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	PF21365	Glycosyl hydrolase family 31 C-terminal domain (Glyco_hydro_31_3rd)	Glycosyl hydrolase family 31 C-terminal domain	Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. This entry represents the 3rd beta sandwich domain.	Domain
A	PF13802	Glycosyl hydrolase 31 N-terminal galactose mutarotase-like domain (Gal_mutarotas_2)	Glycosyl hydrolase 31 N-terminal galactose mutarotase-like domain	This entry represents the first of three common domains found in Glycosyl hydrolase 31 family proteins. It has a galactose mutarotase superfamily fold.	Domain
A	PF01055	Glycosyl hydrolases family 31 TIM-barrel domain (Glyco_hydro_31_2nd)	Glycosyl hydrolases family 31 TIM-barrel domain	Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. This entry corresponds to the second domain of family 31 enzymes and adopts a TIM-barrel fold.	Domain
A	PF17137	Domain of unknown function (DUF5110) (DUF5110)	Domain of unknown function (DUF5110)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Alpha-xylosidase BoGH31A	binding carbohydrate binding hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity alpha-D-xyloside xylohydrolase	biological process involved in interspecies interaction between organisms symbiotic process benefiting host biological process involved in symbiotic interaction carbohydrate metabolic process catabolic process glucan catabolic process hemicellulose metabolic process cell wall organization or biogenesis carbohydrate catabolic process hemicellulose catabolic process primary metabolic process macromolecule catabolic process cell wall macromolecule catabolic process xyloglucan catabolic process biological process involved in interspecies interaction between organisms symbiotic process benefiting host biological process involved in symbiotic interaction carbohydrate metabolic process catabolic process glucan catabolic process hemicellulose metabolic process cell wall organization or biogenesis carbohydrate catabolic process hemicellulose catabolic process primary metabolic process macromolecule catabolic process cell wall macromolecule catabolic process xyloglucan catabolic process polysaccharide metabolic process glucan metabolic process polysaccharide catabolic process xyloglucan metabolic process metabolic process cellular process macromolecule metabolic process cell wall polysaccharide metabolic process cell wall polysaccharide catabolic process cell wall macromolecule metabolic process	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000322	Glycoside hydrolase family 31, TIM barrel domain	Domain
A	IPR048395	Glycosyl hydrolase family 31, C-terminal domain	Domain
A	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A	IPR051816	Glycosyl Hydrolase Family 31	Family
A	IPR033403	Domain of unknown function DUF5110	Domain
A	IPR037524	PA14/GLEYA domain	Domain
A	IPR013780	Glycosyl hydrolase, all-beta	Homologous Superfamily
A	IPR025887	Glycoside hydrolase family 31, N-terminal domain	Domain
A	IPR011013	Galactose mutarotase-like domain superfamily	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.