Protein profile

KP13_05397

N-succinylglutamate 5-semialdehyde dehydrogenase

Genome: KpKP13

Gene: AHE45042.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GN76
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Amino acids 492
Annotations 7
Features 21
PDB binders 9
Druggability 0.901

Overview

Basic information about this protein and its source genome.

Accession
KP13_05397
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45042.1
Status
annotated
Amino acids
492
Structure source
AlphaFold + ColabFold
EC
1.2.1.71
GO
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:0006527 The chemical reactions and pathways resulting in the breakdown of L-arginine. 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. GO:0043824 Catalysis of the reaction: N-succinyl-L-glutamate 5-semialdehyde + H2O + NAD+ = N-succinyl-L-glutamate + 2 H+ + NADH. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
34.409
Human E-value
1.37e-06
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
57.464
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
96.85

Selected Druggability evidence

AlphaFold / UniProt model

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 0.901
Structure A0A0H3GN76
Pocket Pocket 7
P2Rank 0.938
Structure A0A0H3GN76
Pocket Pocket 1
ColabFold model
FPocket 0.601 · Pocket 3
P2Rank 0.923 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 115 / 4744 genomes with a hit
Normalized 0.024

Sequence

Primary amino-acid sequence viewer.

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: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:0006527 The chemical reactions and pathways resulting in the breakdown of L-arginine.
  • 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.
  • GO:0043824 Catalysis of the reaction: N-succinyl-L-glutamate 5-semialdehyde + H2O + NAD+ = N-succinyl-L-glutamate + 2 H+ + NADH.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

21 records
Show feature table
Start End DB Term Name
3 458 PANTHER PTHR11699 ALDEHYDE DEHYDROGENASE-RELATED
2 455 SUPERFAMILY SSF53720 ALDH-like
2 455 InterPro IPR016161 Aldehyde/histidinol dehydrogenase
11 458 Pfam PF00171 Aldehyde dehydrogenase family
11 458 InterPro IPR015590 Aldehyde dehydrogenase domain
7 449 Gene3D G3DSA:3.40.605.10 Aldehyde Dehydrogenase; Chain A, domain 1
7 449 InterPro IPR016162 Aldehyde dehydrogenase, N-terminal
247 437 Gene3D G3DSA:3.40.309.10 Aldehyde Dehydrogenase; Chain A, domain 2
247 437 InterPro IPR016163 Aldehyde dehydrogenase, C-terminal
247 437 FunFam G3DSA:3.40.309.10:FF:000013 N-succinylglutamate 5-semialdehyde dehydrogenase
50 469 CDD cd07095 ALDH_SGSD_AstD
50 469 InterPro IPR017649 Succinylglutamate-semialdehyde dehydrogenase
7 251 FunFam G3DSA:3.40.605.10:FF:000010 N-succinylglutamate 5-semialdehyde dehydrogenase
270 281 ProSitePatterns PS00070 Aldehyde dehydrogenases cysteine active site.
270 281 InterPro IPR016160 Aldehyde dehydrogenase, cysteine active site
242 249 ProSitePatterns PS00687 Aldehyde dehydrogenases glutamic acid active site.
242 249 InterPro IPR029510 Aldehyde dehydrogenase, glutamic acid active site
1 486 Hamap MF_01174 N-succinylglutamate 5-semialdehyde dehydrogenase [astD].
1 486 InterPro IPR017649 Succinylglutamate-semialdehyde dehydrogenase
3 486 NCBIfam TIGR03240 succinylglutamate-semialdehyde dehydrogenase
3 486 InterPro IPR017649 Succinylglutamate-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

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Structural evidence

0 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GN76
AlphaFold — — full sequence — Viewing
ColabFold KP13_05397
ColabFold — — 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
7 0.901

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 26.65 0.916
2 13.62 0.693
3 2.46 0.067
4 1.66 0.028
5 1.53 0.022

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.

35 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
2VS
4NPI
Q83V33 142.1 Da LogP 0.27 TPSA 74.6 ✓ Ro5 ✓ Clean C(=C/C=O)\C=C(\C(=O)O)/O
5OZ
5EK6
G7VCG0 72.1 Da LogP 0.84 TPSA 17.1 ✓ Ro5 ✓ Clean CC(C)C=O
6OA
4OU2
Q83V33 144.1 Da LogP 0.06 TPSA 77.8 ✓ Ro5 ✓ Clean C(/C=C/C=C(/C(=O)O)\O)O
6OD
4I25
Q83V33 141.1 Da LogP -0.33 TPSA 80.4 ✓ Ro5 ✓ Clean C(=C/C=O)\C=C(/C(=O)O)\N
6OH
4I2R
Q83V33 142.1 Da LogP 0.27 TPSA 74.6 ✓ Ro5 ✓ Clean C(=C/C=O)\C=C(/C(=O)O)\O
6UN
5KLL
Q83V33 142.1 Da LogP 0.27 TPSA 74.6 ✓ Ro5 ✓ Clean C(=C/C(=O)C(=O)O)\C=C\O
8YP
5U0L
A1U5W8 156.3 Da LogP 3.33 TPSA 17.1 ✓ Ro5 ✓ Clean CCCCCCCCCC=O
PPI
6FK3
Q72KD3 74.1 Da LogP 0.48 TPSA 37.3 ✓ Ro5 ✓ Clean CCC(=O)O
SIN
3JU8
O50174 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.