2DTJ

Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum

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	ACT_7_1	e2dtjA2	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	ACT_2	e2dtjA1	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	e2dtjB1	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	e2dtjB2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	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	diaminopimelate biosynthetic process oxoacid metabolic process cellular biosynthetic process lipid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process small molecule metabolic process dicarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process diaminopimelate biosynthetic process oxoacid metabolic process cellular biosynthetic process lipid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process small molecule metabolic process dicarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process fatty acid derivative biosynthetic process primary metabolic process fatty acid derivative metabolic process diaminopimelate metabolic process amino acid biosynthetic process biosynthetic process metabolic process cellular process lipid metabolic process serine family amino acid metabolic process alpha-amino acid metabolic process homoserine biosynthetic process L-amino acid biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process proteinogenic amino acid 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 lysine biosynthetic process via diaminopimelate threonine metabolic process threonine biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001048	Aspartate/glutamate/uridylate kinase	Domain
A, B	IPR005260	Aspartate kinase, monofunctional class	Family
A, B	IPR045865	ACT-like domain	Homologous Superfamily
A, B	IPR002912	ACT domain	Domain
A, B	IPR018042	Aspartate kinase, conserved site	Conserved Site
A, B	IPR041740	Aspartokinase catalytic domain	Domain
A, B	IPR054352	Aspartokinase, ACT domain	Domain
A, B	IPR001341	Aspartate kinase	Family
A, B	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.