2QLX

Crystal structure of rhamnose mutarotase RhaU of Rhizobium leguminosarum in complex with L-Rhamnose

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)
A	d2qlxa1	Alpha and beta proteins (a+b)	Ferredoxin-like	Dimeric alpha+beta barrel	automated matches	automated matches	(Rhizobium leguminosarum bv. trifolii ) [TaxId: 386 ],	SCOPe (2.08)
A	d2qlxa2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Rhizobium leguminosarum bv. trifolii ) [TaxId: 386 ],	SCOPe (2.08)
B	d2qlxb1	Alpha and beta proteins (a+b)	Ferredoxin-like	Dimeric alpha+beta barrel	automated matches	automated matches	(Rhizobium leguminosarum bv. trifolii ) [TaxId: 386 ],	SCOPe (2.08)
B	d2qlxb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Rhizobium leguminosarum bv. trifolii ) [TaxId: 386 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Dimeric alpha+beta barrel	8080024	3000089	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Dimeric alpha+beta barrel	8080024	3000089	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	rhaM	e2qlxA1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: rhaM	ECOD (1.6)
B	rhaM	e2qlxB1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: rhaM	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.100	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
B	3.30.70.100	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF05336	L-rhamnose mutarotase (rhaM)	L-rhamnose mutarotase	This family contains L-rhamnose mutarotase which is a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer. In Escherichia coli this enzyme is the product of the rhaM gene (also known as yii ...	This family contains L-rhamnose mutarotase which is a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer. In Escherichia coli this enzyme is the product of the rhaM gene (also known as yiiL). The tertiary structure has been solved, in complex with L-rhamnose, and the catalytic mechanism determined. His22 is the proton donor. The enzyme naturally exists as a dimer.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	L-rhamnose mutarotase	L-rhamnose mutarotase activity isomerase activity racemase and epimerase activity racemase and epimerase activity, acting on carbohydrates and derivatives catalytic activity	rhamnose catabolic process monosaccharide metabolic process carbohydrate metabolic process catabolic process hexose catabolic process carbohydrate catabolic process hexose metabolic process primary metabolic process small molecule metabolic process metabolic process monosaccharide catabolic process small molecule catabolic process rhamnose metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR008000	Rhamnose/fucose mutarotase	Family
A, B	IPR013448	L-rhamnose mutarotase	Family
A, B	IPR011008	Dimeric alpha-beta barrel	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.