Annotations: 6VZ8

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth D]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	SCOP2B (2022-06-29)
A [auth D]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034310	3001790	SCOP2B (2022-06-29)
A [auth D]	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
B [auth E]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	SCOP2B (2022-06-29)
B [auth E]	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
B [auth E]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034310	3001790	SCOP2B (2022-06-29)
E [auth H]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034310	3001790	SCOP2B (2022-06-29)
E [auth H]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	SCOP2B (2022-06-29)
E [auth H]	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
F [auth I]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034310	3001790	SCOP2B (2022-06-29)
F [auth I]	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
F [auth I]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	SCOP2B (2022-06-29)
I [auth L]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034310	3001790	SCOP2B (2022-06-29)
I [auth L]	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
I [auth L]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	SCOP2B (2022-06-29)
J [auth M]	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
J [auth M]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	SCOP2B (2022-06-29)
J [auth M]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034310	3001790	SCOP2B (2022-06-29)
M [auth P]	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
M [auth P]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	SCOP2B (2022-06-29)
M [auth P]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034310	3001790	SCOP2B (2022-06-29)
N [auth Q]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034310	3001790	SCOP2B (2022-06-29)
N [auth Q]	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
N [auth Q]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	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 [auth D]	TPP_enzyme_M	e6vz8D3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: TPP_enzyme_M	ECOD (1.6)
A [auth D]	TPP_enzyme_C	e6vz8D1	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_C	ECOD (1.6)
A [auth D]	TPP_enzyme_N	e6vz8D2	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_N	ECOD (1.6)
B [auth E]	TPP_enzyme_M	e6vz8E1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: TPP_enzyme_M	ECOD (1.6)
B [auth E]	TPP_enzyme_C	e6vz8E3	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_C	ECOD (1.6)
B [auth E]	TPP_enzyme_N	e6vz8E2	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_N	ECOD (1.6)
E [auth H]	TPP_enzyme_M	e6vz8H3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: TPP_enzyme_M	ECOD (1.6)
E [auth H]	TPP_enzyme_C	e6vz8H1	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_C	ECOD (1.6)
E [auth H]	TPP_enzyme_N	e6vz8H2	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_N	ECOD (1.6)
F [auth I]	TPP_enzyme_M	e6vz8I2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: TPP_enzyme_M	ECOD (1.6)
F [auth I]	TPP_enzyme_C	e6vz8I1	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_C	ECOD (1.6)
F [auth I]	TPP_enzyme_N	e6vz8I3	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_N	ECOD (1.6)
I [auth L]	TPP_enzyme_M	e6vz8L1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: TPP_enzyme_M	ECOD (1.6)
I [auth L]	TPP_enzyme_C	e6vz8L2	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_C	ECOD (1.6)
I [auth L]	TPP_enzyme_N	e6vz8L3	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_N	ECOD (1.6)
J [auth M]	TPP_enzyme_M	e6vz8M3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: TPP_enzyme_M	ECOD (1.6)
J [auth M]	TPP_enzyme_C	e6vz8M1	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_C	ECOD (1.6)
J [auth M]	TPP_enzyme_N	e6vz8M2	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_N	ECOD (1.6)
M [auth P]	TPP_enzyme_M	e6vz8P1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: TPP_enzyme_M	ECOD (1.6)
M [auth P]	TPP_enzyme_C	e6vz8P2	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_C	ECOD (1.6)
M [auth P]	TPP_enzyme_N	e6vz8P3	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_N	ECOD (1.6)
N [auth Q]	TPP_enzyme_M	e6vz8Q1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: TPP_enzyme_M	ECOD (1.6)
N [auth Q]	TPP_enzyme_C	e6vz8Q3	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_C	ECOD (1.6)
N [auth Q]	TPP_enzyme_N	e6vz8Q2	A: a/b three-layered sandwiches	X: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	H: Thiamin diphosphate-binding fold (THDP-binding) (From Topology)	T: Thiamin diphosphate-binding fold (THDP-binding)	F: TPP_enzyme_N	ECOD (1.6)
C [auth F]	ALS_ss_C	e6vz8F1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ALS_ss_C	ECOD (1.6)
C [auth F]	ACT_5	e6vz8F2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_5	ECOD (1.6)
D [auth G]	ALS_ss_C	e6vz8G2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ALS_ss_C	ECOD (1.6)
D [auth G]	ACT_5	e6vz8G1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_5	ECOD (1.6)
L [auth O]	ALS_ss_C	e6vz8O1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ALS_ss_C	ECOD (1.6)
L [auth O]	ACT_5	e6vz8O2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_5	ECOD (1.6)
O [auth R]	ALS_ss_C	e6vz8R1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ALS_ss_C	ECOD (1.6)
O [auth R]	ACT_5	e6vz8R2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_5	ECOD (1.6)
G [auth J]	ALS_ss_C	e6vz8J1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ALS_ss_C	ECOD (1.6)
G [auth J]	ACT_5	e6vz8J2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_5	ECOD (1.6)
H [auth K]	ALS_ss_C	e6vz8K1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ALS_ss_C	ECOD (1.6)
H [auth K]	ACT_5	e6vz8K2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_5	ECOD (1.6)
K [auth N]	ALS_ss_C	e6vz8N1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ALS_ss_C	ECOD (1.6)
K [auth N]	ACT_5	e6vz8N2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_5	ECOD (1.6)
P [auth S]	ALS_ss_C	e6vz8S1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ALS_ss_C	ECOD (1.6)
P [auth S]	ACT_5	e6vz8S2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_5	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	PF00205	Thiamine pyrophosphate enzyme, central domain (TPP_enzyme_M)	Thiamine pyrophosphate enzyme, central domain	The central domain of TPP enzymes contains a 2-fold Rossman fold.	Domain
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	PF02775	Thiamine pyrophosphate enzyme, C-terminal TPP binding domain (TPP_enzyme_C)	Thiamine pyrophosphate enzyme, C-terminal TPP binding domain	-	Domain
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	PF02776	Thiamine pyrophosphate enzyme, N-terminal TPP binding domain (TPP_enzyme_N)	Thiamine pyrophosphate enzyme, N-terminal TPP binding domain	-	Domain
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	PF22629	AHAS small subunit-like ACT domain (ACT_AHAS_ss)	AHAS-like ACT domain	This entry represents the ACT domain found at the N-terminal of acetohydroxyacid synthase isozyme III from Escherichia coli and similar sequences.	Domain
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	PF10369	Small subunit of acetolactate synthase (ALS_ss_C)	Small subunit of acetolactate synthase	ALS_ss_C is the C-terminal half of a family of proteins which are the small subunits of acetolactate synthase. Acetolactate synthase is a tetrameric enzyme, containing probably two large and two small subunits, which catalyses the first step in bran ...	ALS_ss_C is the C-terminal half of a family of proteins which are the small subunits of acetolactate synthase. Acetolactate synthase is a tetrameric enzyme, containing probably two large and two small subunits, which catalyses the first step in branched-chain amino acid biosynthesis. This reaction is sensitive to certain herbicides [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	Acetolactate synthase, chloroplastic	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding flavin adenine dinucleotide binding nucleoside phosphate binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding transketolase or transaldolase activity transferase activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding flavin adenine dinucleotide binding nucleoside phosphate binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding transketolase or transaldolase activity transferase activity acetolactate synthase activity catalytic activity vitamin binding thiamine pyrophosphate binding quaternary ammonium group binding sulfur compound binding	response to stimulus response to chemical response to stress response to herbicide response to toxic substance oxoacid metabolic process small molecule biosynthetic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process response to stimulus response to chemical response to stress response to herbicide response to toxic substance oxoacid metabolic process small molecule biosynthetic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process amino acid biosynthetic process biosynthetic process isoleucine biosynthetic process branched-chain amino acid biosynthetic process metabolic process cellular process small molecule metabolic process branched-chain amino acid metabolic process isoleucine metabolic process alpha-amino acid biosynthetic process pyruvate family amino acid metabolic process pyruvate family amino acid biosynthetic process L-amino acid biosynthetic process L-valine biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process proteinogenic amino acid biosynthetic process valine metabolic process	membrane-bounded organelle intracellular anatomical structure plastid intracellular membrane-bounded organelle intracellular organelle cellular anatomical structure plastid stroma organelle chloroplast stroma cytoplasm chloroplast
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	Acetolactate synthase small subunit 2, chloroplastic	enzyme regulator activity acetolactate synthase regulator activity molecular function regulator activity	regulation of molecular function regulation of catalytic activity biological regulation response to decreased oxygen levels response to stimulus response to hypoxia response to stress response to oxygen levels response to abiotic stimulus oxoacid metabolic process small molecule biosynthetic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process regulation of molecular function regulation of catalytic activity biological regulation response to decreased oxygen levels response to stimulus response to hypoxia response to stress response to oxygen levels response to abiotic stimulus oxoacid metabolic process small molecule biosynthetic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process amino acid biosynthetic process biosynthetic process isoleucine biosynthetic process branched-chain amino acid biosynthetic process metabolic process cellular process small molecule metabolic process branched-chain amino acid metabolic process isoleucine metabolic process alpha-amino acid biosynthetic process pyruvate family amino acid metabolic process pyruvate family amino acid biosynthetic process L-amino acid biosynthetic process L-valine biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process proteinogenic amino acid biosynthetic process valine metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle peroxisome microbody cytoplasm intracellular membrane-bounded organelle plastid chloroplast

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR045229	Thiamine pyrophosphate enzyme	Family
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR012001	Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain	Domain
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR000399	TPP-binding enzyme, conserved site	Conserved Site
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR012000	Thiamine pyrophosphate enzyme, central domain	Domain
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR012846	Acetolactate synthase, large subunit, biosynthetic	Family
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR029061	Thiamin diphosphate-binding fold	Homologous Superfamily
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR039368	Acetolactate synthase large subunit, TPP binding domain	Domain
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR029035	DHS-like NAD/FAD-binding domain superfamily	Homologous Superfamily
A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], A [auth D], B [auth E], E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR011766	Thiamine pyrophosphate enzyme, TPP-binding	Domain
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	IPR004789	Acetolactate synthase, small subunit	Family
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	IPR027271	Acetolactate synthase/Transcription factor NikR, C-terminal	Homologous Superfamily
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	IPR045865	ACT-like domain	Homologous Superfamily
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	IPR002912	ACT domain	Domain
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	IPR039557	AHAS, ACT domain	Domain
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	IPR054480	Acetolactate synthase small subunit-like, ACT domain	Domain
C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], C [auth F], D [auth G], G [auth J], H [auth K], K [auth N], L [auth O], O [auth R], P [auth S]	IPR019455	Acetolactate synthase, small subunit, C-terminal	Domain