Annotations: 6U9H

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034310	3001790	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	3001790	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8034305	3001728	SCOP2B (2022-06-29)
B	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	Thiamin diphosphate-binding fold (THDP-binding)	8034310	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)	8034308	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)	8034310	3001790	SCOP2B (2022-06-29)
I [auth L]	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)
J [auth M]	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)	8034310	3001790	SCOP2B (2022-06-29)
M [auth P]	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)
N [auth Q]	SCOP2B Superfamily	Thiamin diphosphate-binding fold (THDP-binding)	8034308	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)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00205	e6u9hA3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF00205	ECOD (1.6)
A	PF02775	e6u9hA1	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: PF02775	ECOD (1.6)
A	PF02776	e6u9hA2	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: PF02776	ECOD (1.6)
B	PF00205	e6u9hB3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF00205	ECOD (1.6)
B	PF02775	e6u9hB1	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: PF02775	ECOD (1.6)
B	PF02776	e6u9hB2	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: PF02776	ECOD (1.6)
E [auth H]	PF00205	e6u9hH3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF00205	ECOD (1.6)
E [auth H]	PF02775	e6u9hH1	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: PF02775	ECOD (1.6)
E [auth H]	PF02776	e6u9hH2	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: PF02776	ECOD (1.6)
F [auth I]	PF00205	e6u9hI3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF00205	ECOD (1.6)
F [auth I]	PF02775	e6u9hI1	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: PF02775	ECOD (1.6)
F [auth I]	PF02776	e6u9hI2	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: PF02776	ECOD (1.6)
I [auth L]	PF00205	e6u9hL2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF00205	ECOD (1.6)
I [auth L]	PF02775	e6u9hL1	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: PF02775	ECOD (1.6)
I [auth L]	PF02776	e6u9hL3	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: PF02776	ECOD (1.6)
J [auth M]	PF00205	e6u9hM3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF00205	ECOD (1.6)
J [auth M]	PF02775	e6u9hM2	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: PF02775	ECOD (1.6)
J [auth M]	PF02776	e6u9hM1	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: PF02776	ECOD (1.6)
M [auth P]	PF00205	e6u9hP3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF00205	ECOD (1.6)
M [auth P]	PF02775	e6u9hP2	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: PF02775	ECOD (1.6)
M [auth P]	PF02776	e6u9hP1	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: PF02776	ECOD (1.6)
N [auth Q]	PF00205	e6u9hQ1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF00205	ECOD (1.6)
N [auth Q]	PF02775	e6u9hQ3	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: PF02775	ECOD (1.6)
N [auth Q]	PF02776	e6u9hQ2	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: PF02776	ECOD (1.6)
C [auth F]	PF10369	e6u9hF2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF10369	ECOD (1.6)
C [auth F]	PF22629	e6u9hF1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF22629	ECOD (1.6)
D [auth G]	PF10369	e6u9hG1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF10369	ECOD (1.6)
D [auth G]	PF22629	e6u9hG2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF22629	ECOD (1.6)
K [auth N]	PF10369	e6u9hN2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF10369	ECOD (1.6)
K [auth N]	PF22629	e6u9hN1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF22629	ECOD (1.6)
L [auth O]	PF10369	e6u9hO1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF10369	ECOD (1.6)
L [auth O]	PF22629	e6u9hO2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF22629	ECOD (1.6)
P [auth S]	PF10369	e6u9hS2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF10369	ECOD (1.6)
P [auth S]	PF22629	e6u9hS1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF22629	ECOD (1.6)
G [auth J]	PF10369	e6u9hJ1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF10369	ECOD (1.6)
G [auth J]	PF22629	e6u9hJ2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF22629	ECOD (1.6)
H [auth K]	PF10369	e6u9hK1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF10369	ECOD (1.6)
H [auth K]	PF22629	e6u9hK2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF22629	ECOD (1.6)
O [auth R]	PF10369	e6u9hR1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF10369	ECOD (1.6)
O [auth R]	PF22629	e6u9hR2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: PF22629	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (utative)
A	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (utative)
B	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (utative)
B	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (utative)
E [auth H]	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (utative)
E [auth H]	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (utative)
F [auth I]	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (utative)
F [auth I]	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (utative)
I [auth L]	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (utative)
I [auth L]	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (utative)
J [auth M]	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (utative)
J [auth M]	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (utative)
M [auth P]	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (utative)
M [auth P]	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (utative)
N [auth Q]	3.40.50.970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains	CATH (utative)
N [auth Q]	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (utative)
C [auth F]	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (utative)
C [auth F]	3.30.70.1150	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT-like. Chain A, domain 2	CATH (utative)
K [auth N]	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (utative)
K [auth N]	3.30.70.1150	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT-like. Chain A, domain 2	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, E [auth H], F [auth I], I [auth L], A, B, 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, B, E [auth H], F [auth I], I [auth L], A, B, 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, B, E [auth H], F [auth I], I [auth L], A, B, 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]	PF01842	ACT domain (ACT)	ACT domain	This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulati ...	This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95 Swiss:P08328, which is inhibited by serine [1]. Aspartokinase EC:2.7.2.4 Swiss:P53553, which is regulated by lysine. Acetolactate synthase small regulatory subunit Swiss:P00894, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1 Swiss:P00439, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51 Swiss:P21203. formyltetrahydrofolate deformylase EC:3.5.1.10, Swiss:P37051, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Swiss:P11585	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]	PF13710	ACT domain (ACT_5)	ACT domain	ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein.	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, B, E [auth H], F [auth I], I [auth L], A, B, 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 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 response to stimulus response to chemical response to stress response to herbicide response to toxic substance oxoacid metabolic 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 isoleucine biosynthetic process organic substance biosynthetic process small molecule metabolic process branched-chain amino acid metabolic process organonitrogen compound metabolic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process amino acid biosynthetic process biosynthetic process branched-chain amino acid biosynthetic process metabolic process cellular process isoleucine metabolic process alpha-amino acid biosynthetic process valine biosynthetic process valine metabolic process	membrane-bounded organelle intracellular anatomical structure plastid cellular anatomical entity intracellular membrane-bounded organelle intracellular organelle 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 cellular biosynthetic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid 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 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 isoleucine biosynthetic process organic substance biosynthetic process small molecule metabolic process branched-chain amino acid metabolic process organonitrogen compound metabolic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process amino acid biosynthetic process biosynthetic process branched-chain amino acid biosynthetic process metabolic process cellular process isoleucine metabolic process alpha-amino acid biosynthetic process valine biosynthetic process valine metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle peroxisome microbody cytoplasm cellular anatomical entity intracellular membrane-bounded organelle plastid chloroplast

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, E [auth H], F [auth I], I [auth L], A, B, E [auth H], F [auth I], I [auth L], J [auth M], M [auth P], N [auth Q]	IPR045229	Thiamine pyrophosphate enzyme	Family
A, B, E [auth H], F [auth I], I [auth L], A, B, 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, B, E [auth H], F [auth I], I [auth L], A, B, 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, B, E [auth H], F [auth I], I [auth L], A, B, 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, B, E [auth H], F [auth I], I [auth L], A, B, 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, B, E [auth H], F [auth I], I [auth L], A, B, 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, B, E [auth H], F [auth I], I [auth L], A, B, 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, B, E [auth H], F [auth I], I [auth L], A, B, 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, B, E [auth H], F [auth I], I [auth L], A, B, 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]	IPR019455	Acetolactate synthase, small subunit, C-terminal	Domain