2GEK

Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF13439	e2gekA3	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PF13439	ECOD (1.6)
A	PF13692	e2gekA2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PF13692	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF13439	Glycosyltransferase Family 4 (Glyco_transf_4)	Glycosyltransferase Family 4	-	Domain
A	PF13692	Glycosyl transferases group 1 (Glyco_trans_1_4)	Glycosyl transferases group 1	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PHOSPHATIDYLINOSITOL MANNOSYLTRANSFERASE (PimA)	glycolipid mannosyltransferase activity glycosyltransferase activity GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity mannosyltransferase activity transferase activity hexosyltransferase activity catalytic activity alpha-1,2-mannosyltransferase activity phosphatidylinositol alpha-mannosyltransferase activity	carbohydrate derivative biosynthetic process membrane lipid metabolic process cellular biosynthetic process glycolipid metabolic process cellular metabolic process liposaccharide metabolic process carbohydrate derivative metabolic process lipid biosynthetic process glycolipid biosynthetic process primary metabolic process organic substance metabolic process biosynthetic process organic substance biosynthetic process cellular lipid metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process cellular biosynthetic process glycolipid metabolic process cellular metabolic process liposaccharide metabolic process carbohydrate derivative metabolic process lipid biosynthetic process glycolipid biosynthetic process primary metabolic process organic substance metabolic process biosynthetic process organic substance biosynthetic process cellular lipid metabolic process metabolic process cellular process membrane lipid biosynthetic process lipid metabolic process phosphatidylinositol metabolic process glycerophospholipid metabolic process phospholipid metabolic process organophosphate metabolic process phosphate-containing compound metabolic process glycerolipid metabolic process phosphorus metabolic process phospholipid biosynthetic process organophosphate biosynthetic process	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR028098	Glycosyltransferase subfamily 4-like, N-terminal domain	Domain

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A	OPM	Monotopic/peripheral	Alpha/Beta monotopic/peripheral	UDP-Glycosyltransferase/glycogen phosphorylase	Glycosyltransferase family 4

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.