Annotations: 1MP4

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1mp4a_	Alpha and beta proteins (a/b)	Nucleotide-diphospho-sugar transferases	Nucleotide-diphospho-sugar transferases	glucose-1-phosphate thymidylyltransferase	RmlA (RfbA)	(Salmonella enterica ) [TaxId: 28901 ],	SCOPe (2.08)
B	d1mp4b_	Alpha and beta proteins (a/b)	Nucleotide-diphospho-sugar transferases	Nucleotide-diphospho-sugar transferases	glucose-1-phosphate thymidylyltransferase	RmlA (RfbA)	(Salmonella enterica ) [TaxId: 28901 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2 Family	Glucose-1-phosphate thymidylyltransferase	8106869	4000694	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Nucleotide-diphospho-sugar transferases	8106870	3000077	SCOP2 (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	NTP_transferase	e1mp4A1	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: NTP_transferase	ECOD (1.6)
B	NTP_transferase	e1mp4B1	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: NTP_transferase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)
B	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	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, B	W224H Variant of S. Enterica RmlA Bound to UDP-Glucose	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding transferase activity nucleotidyltransferase activity catalytic activity glucose-1-phosphate thymidylyltransferase activity transferase activity, transferring phosphorus-containing groups cation binding ion binding metal ion binding	carbohydrate metabolic process polysaccharide biosynthetic process cellular biosynthetic process carbohydrate biosynthetic process cellular metabolic process primary metabolic process macromolecule biosynthetic process extracellular polysaccharide biosynthetic process polysaccharide metabolic process organic substance metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process carbohydrate metabolic process polysaccharide biosynthetic process cellular biosynthetic process carbohydrate biosynthetic process cellular metabolic process primary metabolic process macromolecule biosynthetic process extracellular polysaccharide biosynthetic process polysaccharide metabolic process organic substance metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process extracellular polysaccharide metabolic process macromolecule metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR005835	Nucleotidyl transferase domain	Domain
A, B	IPR029044	Nucleotide-diphospho-sugar transferases	Homologous Superfamily
A, B	IPR005907	Glucose-1-phosphate thymidylyltransferase, short form	Family

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.