7JID

Crystal structure of the L780 UDP-rhamnose synthase from Acanthamoeba polyphaga mimivirus

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	PF04321	e7jidA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF04321	ECOD (1.6)
B	PF04321	e7jidB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF04321	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF04321	RmlD substrate binding domain (RmlD_sub_bind)	RmlD substrate binding domain	L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesised by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsi ...	L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesised by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide [1,2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	UDP-L-Rhamnose Synthase	oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors catalytic activity dTDP-4-dehydrorhamnose reductase activity enzyme regulator activity methionine adenosyltransferase regulator activity molecular function regulator activity	cellular biosynthetic process cellular metabolic process sulfur compound biosynthetic process organic substance metabolic process biosynthetic process S-adenosylmethionine biosynthetic process S-adenosylmethionine metabolic process organic substance biosynthetic process sulfur compound metabolic process metabolic process cellular process carbohydrate derivative biosynthetic process nucleotide-sugar metabolic process carbohydrate derivative metabolic process cellular biosynthetic process cellular metabolic process sulfur compound biosynthetic process organic substance metabolic process biosynthetic process S-adenosylmethionine biosynthetic process S-adenosylmethionine metabolic process organic substance biosynthetic process sulfur compound metabolic process metabolic process cellular process carbohydrate derivative biosynthetic process nucleotide-sugar metabolic process carbohydrate derivative metabolic process primary metabolic process dTDP-rhamnose biosynthetic process nucleobase-containing compound biosynthetic process dTDP-rhamnose metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process nucleobase-containing small molecule metabolic process organic cyclic compound biosynthetic process small molecule metabolic process nucleotide-sugar biosynthetic process carbohydrate metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process macromolecule biosynthetic process extracellular polysaccharide biosynthetic process polysaccharide metabolic process extracellular polysaccharide metabolic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol protein-containing complex catalytic complex methionine adenosyltransferase complex transferase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR029903	RmlD-like substrate binding domain	Domain
A, B	IPR005913	dTDP-4-dehydrorhamnose reductase family	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 R01GM133198.