3UK2

The structure of Pantothenate synthetase from Burkholderia thailandensis

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	d3uk2b1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	automated matches	automated matches	(Burkholderia thailandensis E264 ) [TaxId: 271848 ],	SCOPe (2.08)
B	d3uk2b2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Burkholderia thailandensis E264 ) [TaxId: 271848 ],	SCOPe (2.08)
A	d3uk2a1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	automated matches	automated matches	(Burkholderia thailandensis E264 ) [TaxId: 271848 ],	SCOPe (2.08)
A	d3uk2a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Burkholderia thailandensis E264 ) [TaxId: 271848 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Nucleotidylyl transferase	8079944	3001541	SCOP2B (2022-06-29)
A	SCOP2 Family	Pantothenate synthetase (Pantoate-beta-alanine ligase, PanC)	8079943	4003374	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nucleotidylyl transferase	8079944	3001541	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)
B	Pantoate_ligase_C	e3uk2B3	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: Pantoate_ligase_C	ECOD (1.6)
B	Pantoate_ligase_N	e3uk2B2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Pantoate_ligase_N	ECOD (1.6)
A	Pantoate_ligase_C	e3uk2A3	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: Pantoate_ligase_C	ECOD (1.6)
A	Pantoate_ligase_N	e3uk2A2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Pantoate_ligase_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
B	3.30.1300.10	Alpha Beta	2-Layer Sandwich	Pantoate--beta-alanine Ligase	Chain: A,domain 2	CATH (4.3.0)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
A	3.30.1300.10	Alpha Beta	2-Layer Sandwich	Pantoate--beta-alanine Ligase	Chain: A,domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02569	Pantoate-beta-alanine ligase (Pantoate_ligase)	Pantoate-beta-alanine ligase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Pantothenate synthetase	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 acid-amino acid ligase activity pantoate-beta-alanine ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity	pantothenate metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process modified amino acid biosynthetic process carboxylic acid metabolic process modified amino acid metabolic process vitamin biosynthetic process amide biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process vitamin metabolic process biosynthetic process pantothenate metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process modified amino acid biosynthetic process carboxylic acid metabolic process modified amino acid metabolic process vitamin biosynthetic process amide biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process vitamin metabolic process biosynthetic process pantothenate biosynthetic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process amide metabolic process water-soluble vitamin metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004821	Cytidyltransferase-like domain	Domain
A, B	IPR042176	Pantoate-beta-alanine ligase, C-terminal domain	Homologous Superfamily
A, B	IPR003721	Pantoate-beta-alanine ligase	Family
A, B	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily

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.