Protein profile

PA0130

3-oxopropanoate dehydrogenase

Genome: NC_002516.2

Gene: bauC PA0130 Structure source: AlphaFold UniProt Q9I702
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Amino acids 497
Annotations 7
Features 18
PDB binders 5
Druggability 0.705

Overview

Basic information about this protein and its source genome.

Accession
PA0130
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
bauC PA0130
Status
annotated
Amino acids
497
Structure source
AlphaFold
EC
1.2.1.27
GO
GO:0004491 Catalysis of the reaction: 2-methyl-3-oxopropanoate + CoA + NAD+ = propanoyl-CoA + hydrogencarbonate + NADH + H+. Can also use malonate (3-oxopropanoate) as a substrate. The reaction occurs in two steps with the decarboxylation process preceding CoA-binding. Bicarbonate rather than CO2 is released as a final product. GO:0019483 The chemical reactions and pathways resulting in the formation of beta-alanine (3-aminopropanoic acid), an achiral amino acid and an isomer of alanine. It occurs free (e.g. in brain) and in combination (e.g. in pantothenate) but it is not a constituent of proteins. GO:0006574 The chemical reactions and pathways resulting in the breakdown of L-valine. GO:0006210 The chemical reactions and pathways resulting in the breakdown of thymine, 5-methyluracil, one of the two major pyrimidine bases present (as thymidine) in DNA but not found in RNA other than (as ribothymidine) in transfer RNA, where it is a minor base. 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 (%)
47.035
Human E-value
4.05e-167
Gut microbiome off-target
hit
Essential (DEG)
N
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 0.705
Structure –
Pocket –

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:0004491 Catalysis of the reaction: 2-methyl-3-oxopropanoate + CoA + NAD+ = propanoyl-CoA + hydrogencarbonate + NADH + H+. Can also use malonate (3-oxopropanoate) as a substrate. The reaction occurs in two steps with the decarboxylation process preceding CoA-binding. Bicarbonate rather than CO2 is released as a final product.
  • GO:0019483 The chemical reactions and pathways resulting in the formation of beta-alanine (3-aminopropanoic acid), an achiral amino acid and an isomer of alanine. It occurs free (e.g. in brain) and in combination (e.g. in pantothenate) but it is not a constituent of proteins.
  • GO:0006574 The chemical reactions and pathways resulting in the breakdown of L-valine.
  • GO:0006210 The chemical reactions and pathways resulting in the breakdown of thymine, 5-methyluracil, one of the two major pyrimidine bases present (as thymidine) in DNA but not found in RNA other than (as ribothymidine) in transfer RNA, where it is a minor base.
  • 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.

18 records
Show feature table
Start End DB Term Name
4 481 CDD cd07085 ALDH_F6_MMSDH
4 481 InterPro IPR010061 Methylmalonate-semialdehyde dehydrogenase
273 284 ProSitePatterns PS00070 Aldehyde dehydrogenases cysteine active site.
273 284 InterPro IPR016160 Aldehyde dehydrogenase, cysteine active site
5 481 NCBIfam TIGR01722 CoA-acylating methylmalonate-semialdehyde dehydrogenase
5 481 InterPro IPR010061 Methylmalonate-semialdehyde dehydrogenase
22 458 Gene3D G3DSA:3.40.605.10 Aldehyde Dehydrogenase; Chain A, domain 1
22 458 InterPro IPR016162 Aldehyde dehydrogenase, N-terminal
4 495 PANTHER PTHR43866 MALONATE-SEMIALDEHYDE DEHYDROGENASE
4 495 InterPro IPR010061 Methylmalonate-semialdehyde dehydrogenase
248 450 Gene3D G3DSA:3.40.309.10 Aldehyde Dehydrogenase; Chain A, domain 2
248 450 InterPro IPR016163 Aldehyde dehydrogenase, C-terminal
8 254 FunFam G3DSA:3.40.605.10:FF:000003 Methylmalonate-semialdehyde dehydrogenase [acylating]
3 483 SUPERFAMILY SSF53720 ALDH-like
3 483 InterPro IPR016161 Aldehyde/histidinol dehydrogenase
248 450 FunFam G3DSA:3.40.309.10:FF:000002 Methylmalonate-semialdehyde dehydrogenase (Acylating)
14 477 Pfam PF00171 Aldehyde dehydrogenase family
14 477 InterPro IPR015590 Aldehyde dehydrogenase domain

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 PA0130
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
1 0.705
3 0.283

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.

155 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
6ZU
5L2N
P00352 344.4 Da LogP 3.03 TPSA 73.6 ✓ Ro5 ✓ Clean CC1=C(C(=O)Oc2c1ccc(c2)OS(=O)(=O)C)Cc3ccccc3
6ZY
5L2M
P00352 367.4 Da LogP 4.41 TPSA 63.7 ✓ Ro5 ✓ Clean Cc1c(oc2c1cc3c(c2)OC(=O)C(=C3C)CCC(=O)N4CCCCC4)C
K9P
5AC2
P00352 297.4 Da LogP 4.58 TPSA 40.5 ✓ Ro5 ✓ Clean CCCCCC(=O)N1C[C@H](c2c1cc(c3c2cccc3)O)C
OYA
6X9L
Q87YZ5 128.2 Da LogP 2.55 TPSA 17.1 ✓ Ro5 ✓ Clean CCCCCCCC=O
TXE
5AC2
P00352 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.