Annotations: 3BRK

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth X]	F_UNCLASSIFIED	e3brkX2	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: F_UNCLASSIFIED	ECOD (1.6)
A [auth X]	PF00483	e3brkX1	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: PF00483	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth X]	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)
A [auth X]	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth X]	PF00483	Nucleotidyl transferase (NTP_transferase)	Nucleotidyl transferase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth X]	Glucose-1-phosphate adenylyltransferase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding adenylyltransferase activity glucose-1-phosphate adenylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups	carbohydrate metabolic process glucan biosynthetic process polysaccharide biosynthetic process energy derivation by oxidation of organic compounds cellular biosynthetic process carbohydrate biosynthetic process cellular metabolic process glycogen metabolic process primary metabolic process generation of precursor metabolites and energy glycogen biosynthetic process macromolecule biosynthetic process polysaccharide metabolic process organic substance metabolic process glucan metabolic process carbohydrate metabolic process glucan biosynthetic process polysaccharide biosynthetic process energy derivation by oxidation of organic compounds cellular biosynthetic process carbohydrate biosynthetic process cellular metabolic process glycogen metabolic process primary metabolic process generation of precursor metabolites and energy glycogen biosynthetic process macromolecule biosynthetic process polysaccharide metabolic process organic substance metabolic process glucan metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process energy reserve metabolic process macromolecule metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth X]	IPR011831	Glucose-1-phosphate adenylyltransferase	Family
A [auth X]	IPR005836	ADP-glucose pyrophosphorylase, conserved site	Conserved Site
A [auth X]	IPR023049	Glucose-1-phosphate adenylyltransferase GlgC, bacterial	Family
A [auth X]	IPR011004	Trimeric LpxA-like superfamily	Homologous Superfamily
A [auth X]	IPR005835	Nucleotidyl transferase domain	Domain
A [auth X]	IPR029044	Nucleotide-diphospho-sugar transferases	Homologous Superfamily

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.