5EIO | pdb_00005eio

Crystal structure of LysY from Thermus thermophilus complexed with NADP+ and LysW-gamma-aminoadipic semialdehyde

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	GAPDH-like	8086421	3000043	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	GAPDH-like	8086421	3000043	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	Semialdhyde_dhC_1	e5eioA2	A: a+b two layers	X: FwdE/GAPDH domain-like	H: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)	T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	F: Semialdhyde_dhC_1	ECOD (1.6)
A	Semialdhyde_dh	e5eioA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: Semialdhyde_dh	ECOD (1.6)
B	Semialdhyde_dhC_1	e5eioB2	A: a+b two layers	X: FwdE/GAPDH domain-like	H: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)	T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	F: Semialdhyde_dhC_1	ECOD (1.6)
B	Semialdhyde_dh	e5eioB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: Semialdhyde_dh	ECOD (1.6)
C	TF_Zn_Ribbon_1	e5eioC1	A: few secondary structure elements	X: Rubredoxin-like	H: Rubredoxin-related	T: Rubredoxin-related	F: TF_Zn_Ribbon_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.30.360.10	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B	3.30.360.10	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)
C	2.20.28.160	Mainly Beta	Single Sheet	Rubrerythrin, domain 2		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01118	Semialdehyde dehydrogenase, NAD binding domain (Semialdhyde_dh)	Semialdehyde dehydrogenase, NAD binding domain	This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase	Domain
A, B	PF22698	Semialdehyde dehydrogenase, dimerisation domain (Semialdhyde_dhC_1)	Semialdehyde dehydrogenase, dimerisation domain	This entry represents the dimerisation domain found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) and related sequences not included in Pfam:PF02774 [1-3].	Domain
C	PF21344	Alpha-aminoadipate carrier protein LysW-like, globular domain (Zn_ribbon_LysW)	Alpha-aminoadipate carrier protein LysW-like, globular domain	This domain is found in a group of prokaryotic proteins, including Alpha-aminoadipate carrier protein LysW from Thermus thermophilus. LysW is an amino group-carrier protein that plays an important role in lysine biosynthesis. This globular domain is ...	This domain is found in a group of prokaryotic proteins, including Alpha-aminoadipate carrier protein LysW from Thermus thermophilus. LysW is an amino group-carrier protein that plays an important role in lysine biosynthesis. This globular domain is composed of five beta-strands and adopts a similar structure to members of the zinc ribbon superfamily. It is responsible for the binding of a zinc atom [1-5].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase	NADP+ binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding heterocyclic compound binding NADP binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors N-acetyl-gamma-glutamyl-phosphate reductase activity NADP+ binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding heterocyclic compound binding NADP binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors N-acetyl-gamma-glutamyl-phosphate reductase activity catalytic activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor N-acetyl-gamma-aminoadipyl-phosphate reductase activity NAD binding	L-arginine biosynthetic process oxoacid metabolic process glutamine family amino acid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process glutamine family amino acid metabolic process arginine metabolic process small molecule metabolic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process L-arginine biosynthetic process oxoacid metabolic process glutamine family amino acid biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process glutamine family amino acid metabolic process arginine metabolic process small molecule metabolic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic 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 alpha-amino acid biosynthetic process lysine metabolic process lysine biosynthetic process via aminoadipic acid aspartate family amino acid biosynthetic process aspartate family amino acid metabolic process lysine biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm
C	OrfF	cation binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR037535	[LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase	Family
A, B	IPR050085	N-acetyl-gamma-glutamyl-phosphate reductase	Family
A, B	IPR000706	N-acetyl-gamma-glutamyl-phosphate reductase, type 1	Family
A, B	IPR023013	N-acetyl-gamma-glutamyl-phosphate reductase, active site	Active Site
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR000534	Semialdehyde dehydrogenase, NAD-binding	Domain
C	IPR005906	Lysine biosynthesis protein LysW	Family

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.