Annotations: 3FIG

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	post-HMGL domain-like	8039738	3001285	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Aldolase	8039740	3000445	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Aldolase	8039740	3000445	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	post-HMGL domain-like	8039738	3001285	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	F_UNCLASSIFIED	e3figA3	A: alpha arrays	X: RuvA-C	H: post-HMGL domain-like (From Topology)	T: post-HMGL domain-like	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF08502	e3figA2	A: a+b two layers	X: dsRBD-like	H: 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain (From Topology)	T: 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain	F: PF08502	ECOD (1.6)
A	PF00682	e3figA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00682	ECOD (1.6)
B	F_UNCLASSIFIED	e3figB3	A: alpha arrays	X: RuvA-C	H: post-HMGL domain-like (From Topology)	T: post-HMGL domain-like	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF08502	e3figB1	A: a+b two layers	X: dsRBD-like	H: 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain (From Topology)	T: 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain	F: PF08502	ECOD (1.6)
B	PF00682	e3figB2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00682	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
A	3.30.160.270	Alpha Beta	2-Layer Sandwich	Double Stranded RNA Binding Domain	Alpha-isopropylmalate synthase LeuA, regulatory domain	CATH (4.3.0)
B	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)
B	1.10.287.1400	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
B	1.10.1220.20	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant		CATH (4.3.0)
B	3.30.160.270	Alpha Beta	2-Layer Sandwich	Double Stranded RNA Binding Domain	Alpha-isopropylmalate synthase LeuA, regulatory domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00682	HMGL-like (HMGL-like)	HMGL-like	This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	2-isopropylmalate synthase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding potassium ion binding alkali metal ion binding 2-isopropylmalate synthase activity acyltransferase activity acyltransferase activity, acyl groups converted into alkyl on transfer transferase activity catalytic activity acetyl-CoA C-acetyltransferase activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding potassium ion binding alkali metal ion binding 2-isopropylmalate synthase activity acyltransferase activity acyltransferase activity, acyl groups converted into alkyl on transfer transferase activity catalytic activity acetyl-CoA C-acetyltransferase activity acetyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups acetyl-CoA C-acyltransferase activity C-acyltransferase activity C-acetyltransferase activity manganese ion binding transition metal ion binding zinc ion binding	pyruvate family amino acid metabolic process oxoacid metabolic process pyruvate family amino acid biosynthetic process cellular biosynthetic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process branched-chain amino acid metabolic process pyruvate family amino acid metabolic process oxoacid metabolic process pyruvate family amino acid biosynthetic process cellular biosynthetic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process branched-chain amino acid metabolic process L-leucine metabolic process L-leucine biosynthetic process organonitrogen compound metabolic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process L-amino acid biosynthetic process primary metabolic 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	extracellular region cellular anatomical entity cell periphery plasma membrane membrane intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036230	2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain superfamily	Homologous Superfamily
A, B	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A, B	IPR039371	LeuA, N-terminal catalytic TIM barrel domain	Domain
A, B	IPR000891	Pyruvate carboxyltransferase	Domain
A, B	IPR013709	2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain	Domain
A, B	IPR005668	2-isopropylmalate synthase	Family
A, B	IPR002034	Alpha-isopropylmalate/homocitrate synthase, conserved site	Conserved Site

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.