Annotations: 6UED

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8091502	3001804	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	MurE/MurF N-terminal domain	8091497	3000146	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	PF00132	e6uedA3	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: PF00132	ECOD (1.6)
A	PF04613	e6uedA2	A: a/b three-layered sandwiches	X: MurF and HprK N-domain-like (From Topology)	H: MurF and HprK N-domain-like (From Topology)	T: MurF and HprK N-domain-like	F: PF04613	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1390.10	Alpha Beta	3-Layer(aba) Sandwich	Udp-n-acetylmuramoylalanyl-d-glutamate--2,6- Diaminopimelate Ligase	Chain: A, domain 1	CATH (utative)
A	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00132	Bacterial transferase hexapeptide (six repeats) (Hexapep)	Bacterial transferase hexapeptide (six repeats)	-	Repeat
A	PF04613	UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD (LpxD)	UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	UDP-3-O-acylglucosamine N-acyltransferase	acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity N-acyltransferase activity	glycolipid metabolic process cellular biosynthetic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process organic substance metabolic process organic substance biosynthetic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process glycolipid metabolic process cellular biosynthetic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process organic substance metabolic process organic substance biosynthetic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process cellular metabolic process liposaccharide metabolic process primary metabolic process glycolipid biosynthetic process phospholipid biosynthetic process lipid A metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process cellular lipid metabolic process metabolic process cellular process membrane lipid biosynthetic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011004	Trimeric LpxA-like superfamily	Homologous Superfamily
A	IPR007691	UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD	Family
A	IPR018357	Hexapeptide transferase, conserved site	Conserved Site
A	IPR020573	UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, non-repeat region	Domain
A	IPR001451	Hexapeptide repeat	Repeat

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.