1QZ9 | pdb_00001qz9

The Three Dimensional Structure of Kynureninase from Pseudomonas fluorescens

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1qz9a_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	Cystathionine synthase-like	Kynureninase	(Pseudomonas fluorescens ) [TaxId: 294 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Cystathionine synthase-like	8027726	4000672	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PLP-dependent transferases	8040105	3000954	SCOP2 (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	Bna5	e1qz9A1	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: Bna5	ECOD (1.6)
A	Aminotran_5_N	e1qz9A2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1150.10	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1	Aspartate Aminotransferase, domain 1	CATH (4.3.0)
A	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	KYNURENINASE	vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding anion binding heterocyclic compound binding small molecule binding hydrolase activity, acting on carbon-carbon bonds hydrolase activity, acting on carbon-carbon bonds, in ketonic substances kynureninase activity hydrolase activity catalytic activity	quinolinate metabolic process oxoacid metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process pyridine-containing compound biosynthetic process carboxylic acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process quinolinate biosynthetic process biosynthetic process pyridine-containing compound metabolic process metabolic process cellular process quinolinate metabolic process oxoacid metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process pyridine-containing compound biosynthetic process carboxylic acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process quinolinate biosynthetic process biosynthetic process pyridine-containing compound metabolic process metabolic process cellular process small molecule metabolic process dicarboxylic acid biosynthetic process benzene-containing compound metabolic process aromatic amino acid metabolic process amino acid metabolic process primary metabolic process anthranilate metabolic process monocarboxylic acid metabolic process catabolic process ketone metabolic process organic acid catabolic process alpha-amino acid metabolic process L-kynurenine metabolic process non-proteinogenic amino acid metabolic process carboxylic acid catabolic process ketone catabolic process amino acid catabolic process L-kynurenine catabolic process non-proteinogenic amino acid catabolic process L-amino acid catabolic process L-amino acid metabolic process kynurenine metabolic process alpha-amino acid catabolic process small molecule catabolic process NAD+ biosynthetic process nucleotide biosynthetic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process phosphorus metabolic process NAD+ metabolic process pyridine nucleotide biosynthetic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process nicotinamide nucleotide biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process purine nucleotide biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
A	IPR010111	Kynureninase	Family
A	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A	IPR000653	DegT/DnrJ/EryC1/StrS aminotransferase	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	kynureninase M-CSA #742	Kynureninase is a pyridoxal-5'-phosphate (PLP)-dependent enzyme sourced from Pseudomonas fluorescens that catalyses the hydrolytic cleavage of L-kynurenine to anthranilic acid and L-alanine. This reaction is a key step in the catabolism of L-tryptophan. In fungi and vertebrates, kynurenine is first hydroxylated to 3-hydroxykynurenine - the preferred substrate of kynureninase in those organisms, resulting in 3-hydroxyanthranilate and L-alanine. Kynureninase also plays a role in the biosynthesis of NAD-(P)+. The product of kynureninase is subsequently converted by 3-hydroxyanthranilate-3,4-dioxygenase to quinolinic acid - a precursor of NAD-(P)+. Quinolinic acid is a neurotoxin due to it's agonist effects on N-methyl-D-aspartate receptor. Excessive levels of quinolinic acid have been implicated in a wide range of neurological disorders such as epilepsy, stroke and AIDS related dementia. Therefore, inhibitors of kynureninase are of interest as potential drugs for the treatment of these CNS disorders.	Defined by 5 residues: PHE:A-129ASP:A-201TYR:A-226LYS:A-227ARG:A-375 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.7.1.3 (PDB Primary Data) Search M-CSA Motif + EC 3.7.1.3

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.