1DE6

L-RHAMNOSE ISOMERASE

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	d1de6a_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Xylose isomerase-like	L-rhamnose isomerase	L-rhamnose isomerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1de6d_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Xylose isomerase-like	L-rhamnose isomerase	L-rhamnose isomerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1de6b_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Xylose isomerase-like	L-rhamnose isomerase	L-rhamnose isomerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1de6c_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Xylose isomerase-like	L-rhamnose isomerase	L-rhamnose isomerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	L-rhamnose isomerase	8031332	4003297	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Xylose isomerase-like	8043710	3000560	SCOP2 (2022-06-29)
D	SCOP2B Superfamily	Xylose isomerase-like	8043710	3000560	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Xylose isomerase-like	8043710	3000560	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Xylose isomerase-like	8043710	3000560	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	RhaA	e1de6A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: RhaA	ECOD (1.6)
D	RhaA	e1de6D1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: RhaA	ECOD (1.6)
B	RhaA	e1de6B1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: RhaA	ECOD (1.6)
C	RhaA	e1de6C1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: RhaA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.150	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Divalent-metal-dependent TIM barrel enzymes	CATH (4.3.0)
D	3.20.20.150	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Divalent-metal-dependent TIM barrel enzymes	CATH (4.3.0)
B	3.20.20.150	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Divalent-metal-dependent TIM barrel enzymes	CATH (4.3.0)
C	3.20.20.150	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Divalent-metal-dependent TIM barrel enzymes	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF06134	L-rhamnose isomerase (RhaA) (RhaA)	L-rhamnose isomerase (RhaA)	This family consists of several bacterial L-rhamnose isomerase proteins (EC:5.3.1.14).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	L-RHAMNOSE ISOMERASE	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding rhamnose binding monosaccharide binding carbohydrate binding isomerase activity intramolecular oxidoreductase activity, interconverting aldoses and ketoses L-rhamnose isomerase activity intramolecular oxidoreductase activity cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding rhamnose binding monosaccharide binding carbohydrate binding isomerase activity intramolecular oxidoreductase activity, interconverting aldoses and ketoses L-rhamnose isomerase activity intramolecular oxidoreductase activity catalytic activity zinc ion binding identical protein binding protein binding	monosaccharide metabolic process carbohydrate metabolic process small molecule metabolic process metabolic process cellular process primary metabolic process pentose metabolic process L-lyxose metabolic process rhamnose catabolic process catabolic process hexose catabolic process carbohydrate catabolic process hexose metabolic process monosaccharide catabolic process monosaccharide metabolic process carbohydrate metabolic process small molecule metabolic process metabolic process cellular process primary metabolic process pentose metabolic process L-lyxose metabolic process rhamnose catabolic process catabolic process hexose catabolic process carbohydrate catabolic process hexose metabolic process monosaccharide catabolic process small molecule catabolic process rhamnose metabolic process protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis	cellular anatomical structure intracellular anatomical structure cytoplasm protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036237	Xylose isomerase-like superfamily	Homologous Superfamily
A, B, C, D	IPR050337	L-rhamnose isomerase	Family
A, B, C, D	IPR009308	Rhamnose isomerase	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	L-rhamnose isomerase M-CSA #488	This enzyme interconverts L-rhamnose and L-rhamnulose. In some species, including Escherichia coli, this is the first step in rhamnose catabolism. The enzyme contains two divalent metal ions located at different metal-binding sites within the active site. The enzyme binds the closed ring form of the substrate and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites.	Defined by 9 residues: TRP:A-192 [auth A-193]GLU:A-233 [auth A-234]LYS:A-235 [auth A-236]ASP:A-266 [auth A-267]HIS:A-269 [auth A-270]HIS:A-293 [auth A-294]ASP:A-301 [auth A-302]ASP:A-303 [auth A-304]ASP:A-333 [auth A-334] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.3.1.14 (PDB Primary Data) Search M-CSA Motif + EC 5.3.1.14

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.