Protein profile

PA2080

kynureninase KynU

Genome: NC_002516.2

Gene: PA2080 kynU Structure source: AlphaFold UniProt Q9I235
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Amino acids 416
Annotations 11
Features 17
PDB binders 3
Druggability 0.486

Overview

Basic information about this protein and its source genome.

Accession
PA2080
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2080 kynU
Status
annotated
Amino acids
416
Structure source
AlphaFold
EC
3.7.1.3
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0030429 Catalysis of the reaction: L-kynurenine + H2O = anthranilate + L-alanine + H+. Also acts on 3'-hydroxykynurenine and some other (3-arylcarbonyl)- alanines. GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0043420 OBSOLETE. The chemical reactions and pathways involving anthranilate (2-aminobenzoate). GO:0097053 The chemical reactions and pathways resulting in the breakdown of L-kynurenine, the L-enantiomer of the amino acid kynurenine (3-(2-aminobenzoyl)-alanine). GO:0019441 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-tryptophan into other compounds, including L-kynurenine.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
26.577
Human E-value
5.58e-36
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.486
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

10
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0030429 Catalysis of the reaction: L-kynurenine + H2O = anthranilate + L-alanine + H+. Also acts on 3'-hydroxykynurenine and some other (3-arylcarbonyl)- alanines.
  • GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • GO:0043420 OBSOLETE. The chemical reactions and pathways involving anthranilate (2-aminobenzoate).
  • GO:0097053 The chemical reactions and pathways resulting in the breakdown of L-kynurenine, the L-enantiomer of the amino acid kynurenine (3-(2-aminobenzoyl)-alanine).
  • GO:0019441 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-tryptophan into other compounds, including L-kynurenine.
  • GO:0009435 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions. NAD+ is derived from various sources including vitamin B3.
  • GO:0019805 The chemical reactions and pathways resulting in the formation of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0006569 The chemical reactions and pathways resulting in the breakdown of L-tryptophan.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
77 363 Pfam PF00266 Aminotransferase class-V
77 363 InterPro IPR000192 Aminotransferase class V domain
1 407 PIRSF PIRSF038800 KYNU
1 407 InterPro IPR010111 Kynureninase
1 399 Hamap MF_01970 Kynureninase [kynU].
1 399 InterPro IPR010111 Kynureninase
8 399 NCBIfam TIGR01814 kynureninase
8 399 InterPro IPR010111 Kynureninase
3 400 SUPERFAMILY SSF53383 PLP-dependent transferases
3 400 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
7 404 PANTHER PTHR14084 KYNURENINASE
7 404 InterPro IPR010111 Kynureninase
41 301 FunFam G3DSA:3.40.640.10:FF:000107 Kynureninase
41 301 Gene3D G3DSA:3.40.640.10 -
41 301 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
10 399 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
10 399 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA2080
AlphaFold — — full sequence — Viewing
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
4 0.486
2 0.372
5 0.297

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

57 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
3XH
3E9K
Q16719 195.2 Da LogP 0.21 TPSA 86.6 ✓ Ro5 ✓ Clean c1cc(cc(c1)O)C(=O)NCC(=O)O
P3G
1QZ9
P83788 250.3 Da LogP 1.11 TPSA 46.2 ✓ Ro5 ✓ Clean CCOCCOCCOCCOCCOCC
POA
1M32
P96060 124.0 Da LogP -0.64 TPSA 74.6 ✓ Ro5 ✓ Clean C(C=O)P(=O)(O)O

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.