Protein profile

PA1999

dehydrocarnitine CoA transferase subunit A

Genome: NC_002516.2

Gene: dhcA PA1999 Structure source: AlphaFold UniProt Q9I2B0
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Amino acids 232
Annotations 5
Features 14
PDB binders 4
Druggability 0.557

Overview

Basic information about this protein and its source genome.

Accession
PA1999
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
dhcA PA1999
Status
annotated
Amino acids
232
Structure source
AlphaFold
EC
2.8.3.6
GO
GO:0047569 Catalysis of the reaction: succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA. GO:0042952 A pathway of aromatic compound degradation by ortho-cleavage; one branch converts protocatechuate, derived from phenolic compounds, to beta-ketoadipate, and the other branch converts catechol, generated from various aromatic hydrocarbons, amino aromatics, and lignin monomers, also to beta-ketoadipate. Two additional steps accomplish the conversion of beta-ketoadipate to tricarboxylic acid cycle intermediates. GO:0042413 The chemical reactions and pathways resulting in the breakdown of carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane. GO:0008410 Catalysis of the transfer of a coenzyme A (CoA) group from one compound (donor) to another (acceptor).

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
60.084
Human E-value
8.429999999999999e-94
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 0.557
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

4
  • GO:0047569 Catalysis of the reaction: succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA.
  • GO:0042952 A pathway of aromatic compound degradation by ortho-cleavage; one branch converts protocatechuate, derived from phenolic compounds, to beta-ketoadipate, and the other branch converts catechol, generated from various aromatic hydrocarbons, amino aromatics, and lignin monomers, also to beta-ketoadipate. Two additional steps accomplish the conversion of beta-ketoadipate to tricarboxylic acid cycle intermediates.
  • GO:0042413 The chemical reactions and pathways resulting in the breakdown of carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane.
  • GO:0008410 Catalysis of the transfer of a coenzyme A (CoA) group from one compound (donor) to another (acceptor).

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records
Show feature table
Start End DB Term Name
3 228 Gene3D G3DSA:3.40.1080.10 -
4 218 NCBIfam TIGR02429 3-oxoacid CoA-transferase subunit A
4 218 InterPro IPR012792 3-oxoacid CoA-transferase, subunit A
11 218 Pfam PF01144 Coenzyme A transferase
11 218 InterPro IPR004165 Coenzyme A transferase family I
5 226 SUPERFAMILY SSF100950 NagB/RpiA/CoA transferase-like
5 226 InterPro IPR037171 NagB/RpiA transferase-like
20 35 ProSitePatterns PS01273 Coenzyme A transferases signature 1.
20 35 InterPro IPR004163 Coenzyme A transferase binding site
3 228 FunFam G3DSA:3.40.1080.10:FF:000005 3-oxoacid CoA-transferase subunit A
8 219 SMART SM00882 CoA_trans_3
8 219 InterPro IPR004165 Coenzyme A transferase family I
6 231 PANTHER PTHR13707 KETOACID-COENZYME A TRANSFERASE
6 231 InterPro IPR004165 Coenzyme A transferase family I

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 + 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 PA1999
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 0.557

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.

54 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
4PS
5MZX
Q1D4I4 438.3 Da LogP -0.85 TPSA 191.7 1 viol. ✓ Clean CC(C)(CO[P@](=O)(O)OP(=O)(O)O)[C@H](C(=O)NCCC(=…
8EW
5MZZ
Q1D4I4 144.1 Da LogP 0.49 TPSA 74.6 ✓ Ro5 ✓ Clean CC(=CC(=O)O)CC(=O)O
8EZ
5MZY
Q1D4I4 142.2 Da LogP 1.90 TPSA 37.3 ✓ Ro5 ✓ Clean C[C@H]1CCCC[C@H]1C(=O)O
F8G
6CO9
Q0S7P9 975.8 Da LogP -0.02 TPSA 410.2 3 viol. ✓ Clean C[C@@H]1CCC(=C([C@@]12CCC(=O)O2)C(=O)SCCNC(=O)C…

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.