Protein profile

PA0662

N-acetyl-gamma-glutamyl-phosphate reductase

Genome: NC_002516.2

Gene: PA0662 argC Structure source: AlphaFold UniProt Q9I5Q9
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Amino acids 344
Annotations 9
Features 18
PDB binders 7
Druggability 0.421

Overview

Basic information about this protein and its source genome.

Accession
PA0662
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA0662 argC
Status
annotated
Amino acids
344
Structure source
AlphaFold
EC
1.2.1.38
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0003942 Catalysis of the reaction: N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH + H+. GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. GO:0070401 Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid. GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.421
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0003942 Catalysis of the reaction: N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH + H+.
  • GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
  • GO:0070401 Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
  • GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
  • GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
  • GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
  • GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records
Show feature table
Start End DB Term Name
159 315 Pfam PF02774 Semialdehyde dehydrogenase, dimerisation domain
159 315 InterPro IPR012280 Semialdehyde dehydrogenase, dimerisation domain
2 338 Hamap MF_00150 N-acetyl-gamma-glutamyl-phosphate reductase [argC].
2 338 InterPro IPR000706 N-acetyl-gamma-glutamyl-phosphate reductase, type 1
2 344 PANTHER PTHR32338 N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED
3 330 Gene3D G3DSA:3.40.50.720 -
2 172 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
2 172 InterPro IPR036291 NAD(P)-binding domain superfamily
145 161 ProSitePatterns PS01224 N-acetyl-gamma-glutamyl-phosphate reductase active site.
145 161 InterPro IPR023013 N-acetyl-gamma-glutamyl-phosphate reductase, active site
2 344 NCBIfam TIGR01850 N-acetyl-gamma-glutamyl-phosphate reductase
2 344 InterPro IPR000706 N-acetyl-gamma-glutamyl-phosphate reductase, type 1
148 312 FunFam G3DSA:3.30.360.10:FF:000014 N-acetyl-gamma-glutamyl-phosphate reductase
3 142 SMART SM00859 Semialdhyde_dh_3
3 142 InterPro IPR000534 Semialdehyde dehydrogenase, NAD-binding
3 142 Pfam PF01118 Semialdehyde dehydrogenase, NAD binding domain
150 312 SUPERFAMILY SSF55347 Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
148 312 Gene3D G3DSA:3.30.360.10 Dihydrodipicolinate Reductase; domain 2

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 PA0662
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
2 0.421

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
AZI
2OZP
Q5SH26 42.0 Da LogP 0.87 TPSA 58.7 ✓ Ro5 Alert [N-]=[N+]=[N-]
BTB
2I3A
P9WPZ9 209.2 Da LogP -3.01 TPSA 104.4 ✓ Ro5 ✓ Clean C(CO)N(CCO)C(CO)(CO)CO
MLT
3DR3
P59310 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)O)C(=O)O
MYI
7NOT
P9WPZ9 205.2 Da LogP 1.80 TPSA 62.3 ✓ Ro5 ✓ Clean COc1ccc2c(c1)c(c[nH]2)CC(=O)O
UJQ
7NNR
P9WPZ9 226.2 Da LogP 3.01 TPSA 46.5 ✓ Ro5 ✓ Clean c1ccc2c(c1)C(c3ccccc3O2)C(=O)O
UKE
7NPH
P9WPZ9 193.2 Da LogP 1.53 TPSA 72.6 ✓ Ro5 ✓ Clean COc1ccc2c(c1)nc(o2)C(=O)O
UKK
7NPJ
P9WPZ9 186.2 Da LogP 2.46 TPSA 48.1 ✓ Ro5 Alert c1ccc(cc1)Oc2ccc(cn2)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.