6L2K | pdb_00006l2k

IlvC, a ketol-acid reductoisomerase, from Streptococcus pneumoniae_R49E

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
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)
A	d6l2ka2	All alpha proteins	6-phosphogluconate dehydrogenase C-terminal domain-like	6-phosphogluconate dehydrogenase C-terminal domain-like	automated matches	automated matches	(Streptococcus pneumoniae D39 ) [TaxId: 373153 ],	SCOPe (2.08)
A	d6l2ka1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Streptococcus pneumoniae D39 ) [TaxId: 373153 ],	SCOPe (2.08)
B	d6l2kb2	All alpha proteins	6-phosphogluconate dehydrogenase C-terminal domain-like	6-phosphogluconate dehydrogenase C-terminal domain-like	automated matches	automated matches	(Streptococcus pneumoniae D39 ) [TaxId: 373153 ],	SCOPe (2.08)
B	d6l2kb1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Streptococcus pneumoniae D39 ) [TaxId: 373153 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Ketol-acid reductoisomerase (KARI)-like	8099095	4000106	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	6-phosphogluconate dehydrogenase-like	8099096	3000048	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	6-phosphogluconate dehydrogenase-like	8099096	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	IlvC	e6l2kA1	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: IlvC	ECOD (1.6)
A	IlvN	e6l2kA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: IlvN	ECOD (1.6)
B	IlvC	e6l2kB1	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: IlvC	ECOD (1.6)
B	IlvN	e6l2kB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: IlvN	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF07991	Acetohydroxy acid isomeroreductase, NADPH-binding domain (KARI_N)	Acetohydroxy acid isomeroreductase, NADPH-binding domain	-	Family
A, B	PF01450	Ketol-acid reductoisomerase, C-terminal domain (KARI_C)	Ketol-acid reductoisomerase, C-terminal domain	Ketol-acid reductoisomerase (KARI; EC:1.1.1.86), also known as acetohydroxy acid isomeroreductase (AHIR or AHAIR), catalyses the conversion of acetohydroxy acids into dihydroxy valerates in the second step of the biosynthetic pathway for the essent ...	Ketol-acid reductoisomerase (KARI; EC:1.1.1.86), also known as acetohydroxy acid isomeroreductase (AHIR or AHAIR), catalyses the conversion of acetohydroxy acids into dihydroxy valerates in the second step of the biosynthetic pathway for the essential branched-chain amino acids valine, leucine, and isoleucine [1, 2, 3, 4, 5, 6]. KARI is present only in bacteria, fungi, and plants, but not in animals. KARIs are divided into two classes on the basis of sequence length and oligomerisation state. Class I KARIs are ~340 amino acid residues in length and include all fungal KARIs, whereas class II KARIs are ~490 residues long and include all plant KARIs. Bacterial KARIs can be either class I or class II. KARIs are composed of two types of domains, an N-terminal Rossmann fold domain and one or two C-terminal knotted domains. Two intertwinned knotted domains are required for function, and in the short-chain or class I KARIs, each polypeptide chain has one knotted domain. As a result, dimerization of two monomers forms two complete KARI active sites. In the long-chain or class II KARIs, a duplication of the knotted domain has occurred and, as a result, the protein does not require dimerisation to complete its active site [1, 2, 3, 4, 5, 6]. The alpha-helical KARI C-terminal knotted domain can be described as a six-helix core in which helices coil like cable threads around each other, thus forming a bundle [1, 2, 3, 4, 5].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Ketol-acid reductoisomerase (NADP(+))	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding nucleoside phosphate binding purine nucleotide binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding nucleoside phosphate binding purine nucleotide binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP 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 ketol-acid reductoisomerase activity catalytic activity	pyruvate family amino acid metabolic process oxoacid metabolic process pyruvate family amino acid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process branched-chain amino acid metabolic process small molecule biosynthetic process carboxylic acid metabolic process L-amino acid biosynthetic process primary metabolic process pyruvate family amino acid metabolic process oxoacid metabolic process pyruvate family amino acid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process branched-chain amino acid metabolic process small molecule biosynthetic process carboxylic acid metabolic process L-amino acid biosynthetic process primary metabolic process L-valine biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process branched-chain amino acid biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process alpha-amino acid biosynthetic process valine metabolic process isoleucine biosynthetic process isoleucine metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013023	Ketol-acid reductoisomerase	Family
A, B	IPR014359	Ketol-acid reductoisomerase, prokaryotic	Family
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR000506	Ketol-acid reductoisomerase, C-terminal	Domain
A, B	IPR013116	Ketol-acid reductoisomerase, N-terminal	Domain
A, B	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily	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.