4R37

Crystal structure analysis of LpxA, a UDP-N-acetylglucosamine acyltransferase from Bacteroides fragilis 9343 with UDP-GlcNAc

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)
B	d4r37b_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	automated matches	automated matches	(Bacteroides fragilis NCTC 9343 ) [TaxId: 272559 ],	SCOPe (2.08)
A	d4r37a_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	automated matches	automated matches	(Bacteroides fragilis NCTC 9343 ) [TaxId: 272559 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8063356	3001804	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8063356	3001804	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)
B	Hexapep_2_1	e4r37B1	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: Hexapep_2_1	ECOD (1.6)
A	Hexapep_2_1	e4r37A1	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: Hexapep_2_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)
B	1.20.1180.10	Mainly Alpha	Up-down Bundle	Udp N-acetylglucosamine O-acyltransferase	Domain 2	CATH (4.3.0)
A	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)
A	1.20.1180.10	Mainly Alpha	Up-down Bundle	Udp N-acetylglucosamine O-acyltransferase	Domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00132	Bacterial transferase hexapeptide (six repeats) (Hexapep)	Bacterial transferase hexapeptide (six repeats)	-	Repeat
A, B	PF13720	Udp N-acetylglucosamine O-acyltransferase; Domain 2 (Acetyltransf_11)	Udp N-acetylglucosamine O-acyltransferase; Domain 2	This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyses the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyris ...	This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyses the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Putative acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase	acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity O-acyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	glycolipid metabolic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process liposaccharide metabolic process primary metabolic process glycolipid biosynthetic process glycolipid metabolic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide 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 metabolic process cellular process membrane lipid biosynthetic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR011004	Trimeric LpxA-like superfamily	Homologous Superfamily
A, B	IPR029098	UDP N-acetylglucosamine O-acyltransferase, C-terminal	Domain
A, B	IPR010137	Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase	Family
A, B	IPR037157	UDP-N-acetylglucosamine O-acyltransferase, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR001451	Hexapeptide repeat	Repeat

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.