5YEI | pdb_00005yei

Mechanistic insight into the regulation of Pseudomonas aeruginosa aspartate kinase

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth D]	ACT_7_1	e5yeiD2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_7_1	ECOD (1.6)
A [auth D]	ACT_2	e5yeiD1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_2	ECOD (1.6)
B	ACT_7_1	e5yeiB1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_7_1	ECOD (1.6)
B	ACT_2	e5yeiB2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_2	ECOD (1.6)
C [auth F]	ACT_7_1	e5yeiF2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_7_1	ECOD (1.6)
C [auth F]	ACT_2	e5yeiF1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_2	ECOD (1.6)
E [auth H]	ACT_7_1	e5yeiH1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_7_1	ECOD (1.6)
E [auth H]	ACT_2	e5yeiH2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_2	ECOD (1.6)
D [auth C]	ACT_7_1	e5yeiC3	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_7_1	ECOD (1.6)
D [auth C]	ACT_2	e5yeiC1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_2	ECOD (1.6)
D [auth C]	AA_kinase	e5yeiC2	A: a/b three-layered sandwiches	X: Carbamate kinase-like (From Topology)	H: Carbamate kinase-like (From Topology)	T: Carbamate kinase-like	F: AA_kinase	ECOD (1.6)
F [auth G]	ACT_7_1	e5yeiG1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_7_1	ECOD (1.6)
F [auth G]	ACT_2	e5yeiG2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_2	ECOD (1.6)
F [auth G]	AA_kinase	e5yeiG3	A: a/b three-layered sandwiches	X: Carbamate kinase-like (From Topology)	H: Carbamate kinase-like (From Topology)	T: Carbamate kinase-like	F: AA_kinase	ECOD (1.6)
G [auth A]	ACT_7_1	e5yeiA3	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_7_1	ECOD (1.6)
G [auth A]	ACT_2	e5yeiA2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_2	ECOD (1.6)
G [auth A]	AA_kinase	e5yeiA1	A: a/b three-layered sandwiches	X: Carbamate kinase-like (From Topology)	H: Carbamate kinase-like (From Topology)	T: Carbamate kinase-like	F: AA_kinase	ECOD (1.6)
H [auth E]	ACT_7_1	e5yeiE2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_7_1	ECOD (1.6)
H [auth E]	ACT_2	e5yeiE1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_2	ECOD (1.6)
H [auth E]	AA_kinase	e5yeiE3	A: a/b three-layered sandwiches	X: Carbamate kinase-like (From Topology)	H: Carbamate kinase-like (From Topology)	T: Carbamate kinase-like	F: AA_kinase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth D]	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (4.3.0)
B	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (4.3.0)
C [auth F]	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (4.3.0)
E [auth H]	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (4.3.0)
D [auth C]	3.40.1160.10	Alpha Beta	3-Layer(aba) Sandwich	Carbamate kinase	Acetylglutamate kinase-like	CATH (4.3.0)
D [auth C]	3.30.2130.10	Alpha Beta	2-Layer Sandwich	VC0802-like	VC0802-like	CATH (4.3.0)
F [auth G]	3.40.1160.10	Alpha Beta	3-Layer(aba) Sandwich	Carbamate kinase	Acetylglutamate kinase-like	CATH (4.3.0)
F [auth G]	3.30.2130.10	Alpha Beta	2-Layer Sandwich	VC0802-like	VC0802-like	CATH (4.3.0)
G [auth A]	3.40.1160.10	Alpha Beta	3-Layer(aba) Sandwich	Carbamate kinase	Acetylglutamate kinase-like	CATH (4.3.0)
G [auth A]	3.30.2130.10	Alpha Beta	2-Layer Sandwich	VC0802-like	VC0802-like	CATH (4.3.0)
H [auth E]	3.40.1160.10	Alpha Beta	3-Layer(aba) Sandwich	Carbamate kinase	Acetylglutamate kinase-like	CATH (4.3.0)
H [auth E]	3.30.2130.10	Alpha Beta	2-Layer Sandwich	VC0802-like	VC0802-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth D], B, C [auth F], E [auth H]	PF22468	ACT domain (ACT_9)	ACT domain	This entry represents the ACT domain, which is found twice in Aspartate kinase from Methanocaldococcus jannaschii, the enzyme that catalyses the phosphorylation of aspartic acid [6]. This domain folds as a four-stranded antiparallel sheet with two al ...	This entry represents the ACT domain, which is found twice in Aspartate kinase from Methanocaldococcus jannaschii, the enzyme that catalyses the phosphorylation of aspartic acid [6]. This domain folds as a four-stranded antiparallel sheet with two alpha-helices parallel to the sheet and located on one side of the sheet [1].	Domain
A [auth D], B, C [auth F], E [auth H]	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
D [auth C], F [auth G], G [auth A], H [auth E]	PF22468	ACT domain (ACT_9)	ACT domain	This entry represents the ACT domain, which is found twice in Aspartate kinase from Methanocaldococcus jannaschii, the enzyme that catalyses the phosphorylation of aspartic acid [6]. This domain folds as a four-stranded antiparallel sheet with two al ...	This entry represents the ACT domain, which is found twice in Aspartate kinase from Methanocaldococcus jannaschii, the enzyme that catalyses the phosphorylation of aspartic acid [6]. This domain folds as a four-stranded antiparallel sheet with two alpha-helices parallel to the sheet and located on one side of the sheet [1].	Domain
D [auth C], F [auth G], G [auth A], H [auth E]	PF00696	Amino acid kinase family (AA_kinase)	Amino acid kinase family	-	Family
D [auth C], F [auth G], G [auth A], H [auth E]	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth D], B, C [auth F], E [auth H]	Aspartokinase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding amino acid kinase activity kinase activity aspartate kinase activity phosphotransferase activity, carboxyl group as acceptor transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups	diaminopimelate biosynthetic process oxoacid metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process lipid biosynthetic process carboxylic acid metabolic process fatty acid derivative biosynthetic process primary metabolic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process fatty acid derivative metabolic process diaminopimelate metabolic process amino acid biosynthetic process diaminopimelate biosynthetic process oxoacid metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process lipid biosynthetic process carboxylic acid metabolic process fatty acid derivative biosynthetic process primary metabolic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process fatty acid derivative metabolic process diaminopimelate metabolic process amino acid biosynthetic process biosynthetic process metabolic process cellular process small molecule metabolic process dicarboxylic acid biosynthetic process lipid metabolic process serine family amino acid metabolic process alpha-amino acid metabolic process homoserine biosynthetic process homoserine metabolic process serine family amino acid biosynthetic process alpha-amino acid biosynthetic process lysine metabolic process aspartate family amino acid biosynthetic process aspartate family amino acid metabolic process lysine biosynthetic process L-amino acid biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process lysine biosynthetic process via diaminopimelate proteinogenic amino acid biosynthetic process threonine metabolic process threonine biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol
D [auth C], F [auth G], G [auth A], H [auth E]	Aspartokinase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding amino acid kinase activity kinase activity aspartate kinase activity phosphotransferase activity, carboxyl group as acceptor transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups	diaminopimelate biosynthetic process oxoacid metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process lipid biosynthetic process carboxylic acid metabolic process fatty acid derivative biosynthetic process primary metabolic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process fatty acid derivative metabolic process diaminopimelate metabolic process amino acid biosynthetic process diaminopimelate biosynthetic process oxoacid metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process lipid biosynthetic process carboxylic acid metabolic process fatty acid derivative biosynthetic process primary metabolic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process fatty acid derivative metabolic process diaminopimelate metabolic process amino acid biosynthetic process biosynthetic process metabolic process cellular process small molecule metabolic process dicarboxylic acid biosynthetic process lipid metabolic process serine family amino acid metabolic process alpha-amino acid metabolic process homoserine biosynthetic process homoserine metabolic process serine family amino acid biosynthetic process alpha-amino acid biosynthetic process lysine metabolic process aspartate family amino acid biosynthetic process aspartate family amino acid metabolic process lysine biosynthetic process L-amino acid biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process lysine biosynthetic process via diaminopimelate proteinogenic amino acid biosynthetic process threonine metabolic process threonine biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth D], B, C [auth F], E [auth H]	IPR001048	Aspartate/glutamate/uridylate kinase	Domain
A [auth D], B, C [auth F], E [auth H]	IPR005260	Aspartate kinase, monofunctional class	Family
A [auth D], B, C [auth F], E [auth H]	IPR045865	ACT-like domain	Homologous Superfamily
A [auth D], B, C [auth F], E [auth H]	IPR002912	ACT domain	Domain
A [auth D], B, C [auth F], E [auth H]	IPR018042	Aspartate kinase, conserved site	Conserved Site
A [auth D], B, C [auth F], E [auth H]	IPR041740	Aspartokinase catalytic domain	Domain
A [auth D], B, C [auth F], E [auth H]	IPR054352	Aspartokinase, ACT domain	Domain
A [auth D], B, C [auth F], E [auth H]	IPR001341	Aspartate kinase	Family
A [auth D], B, C [auth F], E [auth H]	IPR036393	Acetylglutamate kinase-like superfamily	Homologous Superfamily
D [auth C], F [auth G], G [auth A], H [auth E]	IPR001048	Aspartate/glutamate/uridylate kinase	Domain
D [auth C], F [auth G], G [auth A], H [auth E]	IPR005260	Aspartate kinase, monofunctional class	Family
D [auth C], F [auth G], G [auth A], H [auth E]	IPR045865	ACT-like domain	Homologous Superfamily
D [auth C], F [auth G], G [auth A], H [auth E]	IPR002912	ACT domain	Domain
D [auth C], F [auth G], G [auth A], H [auth E]	IPR018042	Aspartate kinase, conserved site	Conserved Site
D [auth C], F [auth G], G [auth A], H [auth E]	IPR041740	Aspartokinase catalytic domain	Domain
D [auth C], F [auth G], G [auth A], H [auth E]	IPR054352	Aspartokinase, ACT domain	Domain
D [auth C], F [auth G], G [auth A], H [auth E]	IPR001341	Aspartate kinase	Family
D [auth C], F [auth G], G [auth A], H [auth E]	IPR036393	Acetylglutamate kinase-like superfamily	Homologous Superfamily