Protein profile

PA4483

aspartyl/glutamyl-tRNA amidotransferase subunit A

Genome: NC_002516.2

Gene: gatA PA4483 Structure source: Experimental + AlphaFold UniProt Q9HVT8
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Amino acids 484
Annotations 6
Features 14
PDB binders 4
Druggability 0.381

Overview

Basic information about this protein and its source genome.

Accession
PA4483
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
gatA PA4483
Status
annotated
Amino acids
484
Structure source
Experimental + AlphaFold
EC
6.3.5.7
GO
GO:0030956 A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0050567 Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP. GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
42.403
Human E-value
7.980000000000002e-57
Gut microbiome off-target
hit
Essential (DEG)
Y
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 0.381
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

5
  • GO:0030956 A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0050567 Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP.
  • GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
  • 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.

14 records
Show feature table
Start End DB Term Name
3 480 PANTHER PTHR11895 TRANSAMIDASE
3 480 InterPro IPR000120 Amidase
23 464 Pfam PF01425 Amidase
23 464 InterPro IPR023631 Amidase signature domain
3 481 SUPERFAMILY SSF75304 Amidase signature (AS) enzymes
3 481 InterPro IPR036928 Amidase signature (AS) superfamily
150 181 ProSitePatterns PS00571 Amidases signature.
150 181 InterPro IPR020556 Amidase, conserved site
12 473 NCBIfam TIGR00132 Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatA
12 473 InterPro IPR004412 Glutamyl-tRNA(Gln) amidotransferase A subunit
10 475 Hamap MF_00120 Glutamyl-tRNA(Gln) amidotransferase subunit A [gatA].
10 475 InterPro IPR004412 Glutamyl-tRNA(Gln) amidotransferase A subunit
1 484 Gene3D G3DSA:3.90.1300.10 Amidase signature (AS) domain
1 484 InterPro IPR036928 Amidase signature (AS) superfamily

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

1 + 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 4WJ3
X-ray 3.70 Å A,D,G,J
100.0% 1-484
PDBe RCSB PDBj File
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AlphaFold PA4483
AlphaFold — — full sequence — Loaded
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Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 15.04 0.743
2 2.29 0.058
3 1.72 0.03
4 1.72 0.03
5 0.94 0.005

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.

54 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
CXS
4YJI
C3UWD1 221.3 Da LogP 1.19 TPSA 66.4 ✓ Ro5 ✓ Clean C1CCC(CC1)NCCCS(=O)(=O)O
GJY
6DII
Q7XJJ7 344.5 Da LogP 7.38 TPSA 26.3 1 viol. ✓ Clean CC/C=C\C/C=C\C/C=C\CCCCCCCC[P@](=O)(OC)F
TYL
4YJI
C3UWD1 151.2 Da LogP 1.35 TPSA 49.3 ✓ Ro5 ✓ Clean CC(=O)Nc1ccc(cc1)O
UNU
3A1I
Q7DKE4 121.1 Da LogP 0.79 TPSA 43.1 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)N

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.