Protein profile

KP13_04993

N-succinylglutamate 5-semialdehyde dehydrogenase

Genome: KpKP13

Gene: AHE44832.1 astD Structure source: AlphaFold + ColabFold UniProt A0A0H3GMM3
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Amino acids 488
Annotations 7
Features 21
PDB binders 8
Druggability 0.668

Overview

Basic information about this protein and its source genome.

Accession
KP13_04993
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE44832.1 astD
Status
annotated
Amino acids
488
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 (%)
34.568
Human E-value
4.95e-06
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
55.694
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
97.35

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 0.668
Structure A0A0H3GMM3
Pocket Pocket 2
P2Rank 0.915
Structure A0A0H3GMM3
Pocket Pocket 1
ColabFold model
FPocket 0.785 · Pocket 2
P2Rank 0.883 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 114 / 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
4 488 Hamap MF_01174 N-succinylglutamate 5-semialdehyde dehydrogenase [astD].
4 488 InterPro IPR017649 Succinylglutamate-semialdehyde dehydrogenase
250 439 FunFam G3DSA:3.40.309.10:FF:000013 N-succinylglutamate 5-semialdehyde dehydrogenase
12 460 Pfam PF00171 Aldehyde dehydrogenase family
12 460 InterPro IPR015590 Aldehyde dehydrogenase domain
250 439 Gene3D G3DSA:3.40.309.10 Aldehyde Dehydrogenase; Chain A, domain 2
250 439 InterPro IPR016163 Aldehyde dehydrogenase, C-terminal
5 457 SUPERFAMILY SSF53720 ALDH-like
5 457 InterPro IPR016161 Aldehyde/histidinol dehydrogenase
4 460 PANTHER PTHR11699 ALDEHYDE DEHYDROGENASE-RELATED
245 252 ProSitePatterns PS00687 Aldehyde dehydrogenases glutamic acid active site.
245 252 InterPro IPR029510 Aldehyde dehydrogenase, glutamic acid active site
10 451 Gene3D G3DSA:3.40.605.10 Aldehyde Dehydrogenase; Chain A, domain 1
10 451 InterPro IPR016162 Aldehyde dehydrogenase, N-terminal
10 255 FunFam G3DSA:3.40.605.10:FF:000010 N-succinylglutamate 5-semialdehyde dehydrogenase
53 471 CDD cd07095 ALDH_SGSD_AstD
53 471 InterPro IPR017649 Succinylglutamate-semialdehyde dehydrogenase
273 284 ProSitePatterns PS00070 Aldehyde dehydrogenases cysteine active site.
273 284 InterPro IPR016160 Aldehyde dehydrogenase, cysteine active site
6 487 NCBIfam TIGR03240 succinylglutamate-semialdehyde dehydrogenase
6 487 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_A0A0H3GMM3
AlphaFold — — full sequence — Viewing
ColabFold KP13_04993
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
2 0.668
1 0.212

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 22.62 0.882
2 13.96 0.706
3 2.43 0.066
4 1.23 0.012

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

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
7PE
2WOX
Q9HTJ1 310.4 Da LogP 0.10 TPSA 75.6 ✓ Ro5 ✓ Clean CCOCCOCCOCCOCCOCCOCCO
8YP
5U0L
A1U5W8 156.3 Da LogP 3.33 TPSA 17.1 ✓ Ro5 ✓ Clean CCCCCCCCCC=O
DTT
4CBB
Q9HTJ1 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CS)O)O)S
IAC
5IUW
Q88BC5 175.2 Da LogP 1.79 TPSA 53.1 ✓ Ro5 ✓ Clean c1ccc2c(c1)c(c[nH]2)CC(=O)O
PE4
4CAZ
Q9HTJ1 354.4 Da LogP 0.11 TPSA 84.8 ✓ Ro5 ✓ Clean CCOCCOCCOCCOCCOCCOCCOCCO
SIN
3JU8
O50174 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)O
TOE
2XDR
Q9HTJ1 164.2 Da LogP -0.34 TPSA 47.9 ✓ Ro5 ✓ Clean COCCOCCOCCO
TXE
4CAZ
Q9HTJ1 667.5 Da LogP -2.95 TPSA 317.6 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…

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.