Protein profile

PA0299

aminotransferase

Genome: NC_002516.2

Gene: spuC PA0299 Structure source: Experimental + AlphaFold UniProt Q9I6J2
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Amino acids 456
Annotations 8
Features 18
PDB binders 3
Druggability 0.777

Overview

Basic information about this protein and its source genome.

Accession
PA0299
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
spuC PA0299
Status
annotated
Amino acids
456
Structure source
Experimental + AlphaFold
EC
2.6.1.113
GO
GO:0004015 Catalysis of the reaction: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate. 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:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid. GO:0009102 The chemical reactions and pathways resulting in the formation of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid. GO:0009448 The chemical reactions and pathways involving gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms. GO:0009447 The chemical reactions and pathways resulting in the breakdown of putrescine, 1,4-diaminobutane; putrescine is the metabolic precursor of spermidine and spermine.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
45.238
Human E-value
5.88e-06
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 0.777
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • GO:0004015 Catalysis of the reaction: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate.
  • 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:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
  • GO:0009102 The chemical reactions and pathways resulting in the formation of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
  • GO:0009448 The chemical reactions and pathways involving gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms.
  • GO:0009447 The chemical reactions and pathways resulting in the breakdown of putrescine, 1,4-diaminobutane; putrescine is the metabolic precursor of spermidine and spermine.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records
Show feature table
Start End DB Term Name
13 447 CDD cd00610 OAT_like
13 447 InterPro IPR005814 Aminotransferase class-III
11 449 SUPERFAMILY SSF53383 PLP-dependent transferases
11 449 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
22 447 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
22 447 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
71 345 FunFam G3DSA:3.40.640.10:FF:000014 Adenosylmethionine-8-amino-7-oxononanoate aminotransferase, probable
37 446 Pfam PF00202 Aminotransferase class-III
37 446 InterPro IPR005814 Aminotransferase class-III
259 296 ProSitePatterns PS00600 Aminotransferases class-III pyridoxal-phosphate attachment site.
259 296 InterPro IPR005814 Aminotransferase class-III
143 450 PIRSF PIRSF000521 Transaminase_4ab_Lys_Orn
143 450 InterPro IPR005814 Aminotransferase class-III
35 154 PIRSF PIRSF000521 Transaminase_4ab_Lys_Orn
35 154 InterPro IPR005814 Aminotransferase class-III
33 452 PANTHER PTHR43094 AMINOTRANSFERASE
71 345 Gene3D G3DSA:3.40.640.10 -
71 345 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major 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

4 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 9J50
X-ray 2.80 Å A,B,C,D
98.9% 4-454
PDBe RCSB PDBj File
Viewing
PDB 9J4Z
X-ray 3.40 Å A,B,C,D
98.9% 4-454
PDBe RCSB PDBj File
Loaded
PDB 9J2K
X-ray 1.76 Å A,B
93.4% 22-447
PDBe RCSB PDBj File
Loaded
PDB 9J4Y
X-ray 2.50 Å A,B,C,D,E,F,G,H
93.4% 22-447
PDBe RCSB PDBj File
Loaded
AlphaFold PA0299
AlphaFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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.

50 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
BEN
4E3Q
F2XBU9 120.2 Da LogP 0.97 TPSA 49.9 ✓ Ro5 ✓ Clean [H]/N=C(\c1ccccc1)/N
PMP
7B4J
A0A2W0F5X5 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
SIN
7B4J
A0A2W0F5X5 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=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.