3C1N

Crystal Structure of Allosteric Inhibition Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-threonine

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	d3c1na1	Alpha and beta proteins (a/b)	Carbamate kinase-like	Carbamate kinase-like	PyrH-like	automated matches	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)
A	d3c1na2	Alpha and beta proteins (a+b)	Ferredoxin-like	ACT-like	automated matches	automated matches	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)
B	d3c1nb1	Alpha and beta proteins (a/b)	Carbamate kinase-like	Carbamate kinase-like	PyrH-like	automated matches	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)
B	d3c1nb2	Alpha and beta proteins (a+b)	Ferredoxin-like	ACT-like	automated matches	automated matches	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)
C	d3c1nc1	Alpha and beta proteins (a/b)	Carbamate kinase-like	Carbamate kinase-like	PyrH-like	automated matches	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)
C	d3c1nc2	Alpha and beta proteins (a+b)	Ferredoxin-like	ACT-like	automated matches	automated matches	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)
D	d3c1nd1	Alpha and beta proteins (a/b)	Carbamate kinase-like	Carbamate kinase-like	PyrH-like	automated matches	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)
D	d3c1nd2	Alpha and beta proteins (a+b)	Ferredoxin-like	ACT-like	automated matches	automated matches	(Methanocaldococcus jannaschii ) [TaxId: 2190 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ACT-like	8042364	3000006	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Carbamate kinase-like	8042362	3001310	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Carbamate kinase-like	8042362	3001310	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	ACT-like	8042364	3000006	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ACT-like	8042364	3000006	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Carbamate kinase-like	8042362	3001310	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	ACT-like	8042364	3000006	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Carbamate kinase-like	8042362	3001310	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	ACT_7_1	e3c1nA4	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	AA_kinase	e3c1nA6	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)
B	ACT_7_1	e3c1nB4	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	AA_kinase	e3c1nB6	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)
C	ACT_7_1	e3c1nC4	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	AA_kinase	e3c1nC6	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)
D	ACT_7_1	e3c1nD4	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	AA_kinase	e3c1nD6	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	3.40.1160.10	Alpha Beta	3-Layer(aba) Sandwich	Carbamate kinase	Acetylglutamate kinase-like	CATH (4.3.0)
A	3.30.2130.10	Alpha Beta	2-Layer Sandwich	VC0802-like	VC0802-like	CATH (4.3.0)
B	3.40.1160.10	Alpha Beta	3-Layer(aba) Sandwich	Carbamate kinase	Acetylglutamate kinase-like	CATH (4.3.0)
B	3.30.2130.10	Alpha Beta	2-Layer Sandwich	VC0802-like	VC0802-like	CATH (4.3.0)
C	3.40.1160.10	Alpha Beta	3-Layer(aba) Sandwich	Carbamate kinase	Acetylglutamate kinase-like	CATH (4.3.0)
C	3.30.2130.10	Alpha Beta	2-Layer Sandwich	VC0802-like	VC0802-like	CATH (4.3.0)
D	3.40.1160.10	Alpha Beta	3-Layer(aba) Sandwich	Carbamate kinase	Acetylglutamate kinase-like	CATH (4.3.0)
D	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, B, C, D	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, B, C, D	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, B, C, D	Probable aspartokinase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound 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	serine family amino acid metabolic process oxoacid metabolic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process homoserine biosynthetic process small molecule metabolic process small molecule biosynthetic process carboxylic acid metabolic process L-amino acid biosynthetic process primary metabolic process L-amino acid metabolic process serine family amino acid metabolic process oxoacid metabolic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process homoserine biosynthetic process small molecule metabolic process small molecule biosynthetic 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 proteinogenic amino acid biosynthetic process metabolic process cellular 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 dicarboxylic acid metabolic process diaminopimelate metabolic process fatty acid derivative metabolic process lysine biosynthetic process via diaminopimelate lipid metabolic 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, B, C, D	IPR001048	Aspartate/glutamate/uridylate kinase	Domain
A, B, C, D	IPR005260	Aspartate kinase, monofunctional class	Family
A, B, C, D	IPR045865	ACT-like domain	Homologous Superfamily
A, B, C, D	IPR002912	ACT domain	Domain
A, B, C, D	IPR018042	Aspartate kinase, conserved site	Conserved Site
A, B, C, D	IPR041746	Lysine-sensitive aspartokinase catalytic domain	Domain
A, B, C, D	IPR054352	Aspartokinase, ACT domain	Domain
A, B, C, D	IPR001341	Aspartate kinase	Family
A, B, C, D	IPR036393	Acetylglutamate kinase-like 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.