Protein profile

PA0898

N-succinylglutamate 5-semialdehyde dehydrogenase

Genome: NC_002516.2

Gene: aruD astD PA0898 Structure source: Experimental + AlphaFold UniProt O50174
Export view
Amino acids 488
Annotations 7
Features 21
PDB binders 8
Druggability 0.638

Overview

Basic information about this protein and its source genome.

Accession
PA0898
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
aruD astD PA0898
Status
annotated
Amino acids
488
Structure source
Experimental + AlphaFold
EC
1.2.1.71
GO
GO:0043824 Catalysis of the reaction: N-succinyl-L-glutamate 5-semialdehyde + H2O + NAD+ = N-succinyl-L-glutamate + 2 H+ + NADH. GO:0006527 The chemical reactions and pathways resulting in the breakdown of L-arginine. GO:0019544 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-arginine into other compounds, including L-glutamate. GO:0019545 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-arginine into other compounds, including succinate. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
41.837
Human E-value
2.9e-10
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 0.638
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MMSTHYIAGQWLAGQGETLESLDPVGQGVVWSGRGADATQVDAAVCAAREAFPAWARRPLEQRIELLERFAATLKSRADELARVIGEETGKPLWESATEVTSMVNKVAISVQAFRERTGEKSGPLADATAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNCVVFKPSELTPKVAELTLKAWIQAGLPAGVLNLVQGGRETGVALAAHRGLDGLFFTGSSRTGNLLHSQFGGQPQKILALEMGGNNPLVVEEVADLDAAVYTIIQSAFISAGQRCTCARRLLVPQGAWGDALLARLVAVSATLRVGRFDEQPAPFMGAVISLSAAEHLLKAQEHLIGKGAQPLLAMTQPIDGAALLTPGILDVSAVAERPDEEFFGPLLQVIRYSDFAAAIREANATQYGLAAGLLSDSRERFEQFLVESRAGIVNWNKQLTGAASSAPFGGIGASGNHRPSAYYAADYCAYPVASLESPSVSLPATLTPGISL

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0043824 Catalysis of the reaction: N-succinyl-L-glutamate 5-semialdehyde + H2O + NAD+ = N-succinyl-L-glutamate + 2 H+ + NADH.
  • GO:0006527 The chemical reactions and pathways resulting in the breakdown of L-arginine.
  • GO:0019544 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-arginine into other compounds, including L-glutamate.
  • GO:0019545 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-arginine into other compounds, including succinate.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • 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.

21 records
Show feature table
Start End DB Term Name
11 462 Pfam PF00171 Aldehyde dehydrogenase family
11 462 InterPro IPR015590 Aldehyde dehydrogenase domain
244 251 ProSitePatterns PS00687 Aldehyde dehydrogenases glutamic acid active site.
244 251 InterPro IPR029510 Aldehyde dehydrogenase, glutamic acid active site
40 471 CDD cd07095 ALDH_SGSD_AstD
40 471 InterPro IPR017649 Succinylglutamate-semialdehyde dehydrogenase
249 439 Gene3D G3DSA:3.40.309.10 Aldehyde Dehydrogenase; Chain A, domain 2
249 439 InterPro IPR016163 Aldehyde dehydrogenase, C-terminal
9 451 Gene3D G3DSA:3.40.605.10 Aldehyde Dehydrogenase; Chain A, domain 1
9 451 InterPro IPR016162 Aldehyde dehydrogenase, N-terminal
3 488 Hamap MF_01174 N-succinylglutamate 5-semialdehyde dehydrogenase [astD].
3 488 InterPro IPR017649 Succinylglutamate-semialdehyde dehydrogenase
4 457 SUPERFAMILY SSF53720 ALDH-like
4 457 InterPro IPR016161 Aldehyde/histidinol dehydrogenase
249 439 FunFam G3DSA:3.40.309.10:FF:000013 N-succinylglutamate 5-semialdehyde dehydrogenase
5 487 NCBIfam TIGR03240 succinylglutamate-semialdehyde dehydrogenase
5 487 InterPro IPR017649 Succinylglutamate-semialdehyde dehydrogenase
272 283 ProSitePatterns PS00070 Aldehyde dehydrogenases cysteine active site.
272 283 InterPro IPR016160 Aldehyde dehydrogenase, cysteine active site
3 460 PANTHER PTHR11699 ALDEHYDE DEHYDROGENASE-RELATED
9 254 FunFam G3DSA:3.40.605.10:FF:000010 N-succinylglutamate 5-semialdehyde dehydrogenase

3D Structure

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

3D visualization script Full viewer

Loading 3D structure...

Legend High Medium Low

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 3JU8
X-ray 1.82 Å A,B
99.6% 1-486
PDBe RCSB PDBj File
Viewing
AlphaFold PA0898
AlphaFold — — full sequence — Loaded
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
1 0.638

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 47.59 0.976
2 1.54 0.023
3 1.35 0.015
4 0.93 0.004

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.

58 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

Show only:
Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
SIN
3JU8 1.82 Å Open crystal
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.