1YON

Escherichia coli ketopantoate reductase in complex with 2-monophosphoadenosine-5'-diphosphate

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1yona1	All alpha proteins	6-phosphogluconate dehydrogenase C-terminal domain-like	6-phosphogluconate dehydrogenase C-terminal domain-like	Ketopantoate reductase PanE	Ketopantoate reductase PanE	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1yona2	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	6-phosphogluconate dehydrogenase-like, N-terminal domain	Ketopantoate reductase PanE	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	6-phosphogluconate dehydrogenase-like	8001177	3000048	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)
A	ApbA_C	e1yonA1	A: alpha arrays	X: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	H: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	T: 6-phosphogluconate dehydrogenase C-terminal domain-like	F: ApbA_C	ECOD (1.6)
A	ApbA	e1yonA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: ApbA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	1.10.1040.10	Mainly Alpha	Orthogonal Bundle	N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02558	Ketopantoate reductase PanE/ApbA (ApbA)	Ketopantoate reductase PanE/ApbA	-	Family
A	PF08546	Ketopantoate reductase PanE/ApbA C terminal (ApbA_C)	Ketopantoate reductase PanE/ApbA C terminal	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	2-dehydropantoate 2-reductase	binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors 2-dehydropantoate 2-reductase activity catalytic activity	oxoacid metabolic process cellular biosynthetic process vitamin biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process amide metabolic process water-soluble vitamin metabolic process pantothenate metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process oxoacid metabolic process cellular biosynthetic process vitamin biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process amide metabolic process water-soluble vitamin metabolic process pantothenate metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process amide biosynthetic process vitamin metabolic process cellular modified amino acid metabolic process biosynthetic process cellular modified amino acid biosynthetic process pantothenate biosynthetic process metabolic process cellular process monocarboxylic acid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR003710	Ketopantoate reductase ApbA/PanE	Family
A	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR013328	6-phosphogluconate dehydrogenase, domain 2	Homologous Superfamily
A	IPR013752	Ketopantoate reductase, C-terminal domain	Domain
A	IPR013332	Ketopantoate reductase, N-terminal domain	Domain
A	IPR050838	Ketopantoate reductase	Family
A	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	2-dehydropantoate 2-reductase M-CSA #721	Ketopantoate reductase (KPR), isolated from Escherichia coli, catalyses the reduction of ketopantoate by NADPH to form pantoate and NADP+. This is the second reaction in the pathway for the biosynthesis of pantothenate (vitamin B5). KPR is a member of the 6-phosphogluconate dehydrogenase superfamily. The reaction proceeds by a sequential ordered bi:bi kinetic mechanism, with NADPH binding first, followed by a conformational change and the binding of ketopantoate. After the reaction NADP+ dissociates first, followed by pantoate.	Defined by 1 residue: LYS:A-176 \| Explore in 3D: M-CSA Motif Definition At least 2 residues must be present to support Structure Motif searching. EC: 1.1.1.169 (PDB Primary Data)

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.