Protein profile

PA5445

coenzyme A transferase

Genome: NC_002516.2

Gene: PA5445 Structure source: Experimental + AlphaFold UniProt Q9HTC2
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Amino acids 497
Annotations 6
Features 19
PDB binders 3
Druggability 0.72

Overview

Basic information about this protein and its source genome.

Accession
PA5445
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5445
Status
annotated
Amino acids
497
Structure source
Experimental + AlphaFold
GO
GO:0008775 Catalysis of the reaction: acyl-CoA + acetate = a fatty acid anion + acetyl-CoA. GO:0003986 Catalysis of the reaction: acetyl-CoA + H2O = acetate + CoA + H+. GO:0006083 The chemical reactions and pathways involving acetate, the anion of acetic acid. GO:0006084 The chemical reactions and pathways involving acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis. GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. 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
No hit
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 0.72
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MYRDRVRLPSLLDKVMSAAEAADLIQDGMTVGMSGFTRAGEAKAVPQALAMRAKERPLRISLMTGASLGNDLDKQLTEAGVLARRMPFQVDSTLRKAINAGEVMFIDQHLSETVEQLRNHQLKLPDIAVIEAAAITEQGHIVPTTSVGNSASFAIFAKQVIVEINLAHSTNLEGLHDIYIPTYRPTRTPIPLTRVDDRIGSTAIPIPPEKIVAIVINDQPDSPSTVLPPDGETQAIANHLIDFFKREVDAGRMSNSLGPLQAGIGSIANAVMCGLIESPFENLTMYSEVLQDSTFDLIDAGKLRFASGSSITLSPRRNADVFGNLERYKDKLVLRPQEISNHPEVVRRLGIIGINTALEFDIYGNVNSTHVGGTKMMNGIGGSGDFARNAHLAIFVTKSIAKGGNISSVVPMVSHVDHTEHDVDILVTEQGLADLRGLAPRERARVIIENCVHPSYQAPLLDYFEAACAKGGHTPHLLREALAWHLNLEERGHMLAG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • GO:0008775 Catalysis of the reaction: acyl-CoA + acetate = a fatty acid anion + acetyl-CoA.
  • GO:0003986 Catalysis of the reaction: acetyl-CoA + H2O = acetate + CoA + H+.
  • GO:0006083 The chemical reactions and pathways involving acetate, the anion of acetic acid.
  • GO:0006084 The chemical reactions and pathways involving acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis.
  • GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
  • 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.

19 records
Show feature table
Start End DB Term Name
225 494 SUPERFAMILY SSF100950 NagB/RpiA/CoA transferase-like
225 494 InterPro IPR037171 NagB/RpiA transferase-like
336 476 FunFam G3DSA:3.40.1080.20:FF:000001 Acetyl-CoA hydrolase Ach1
13 494 NCBIfam TIGR03458 succinate CoA transferase
13 494 InterPro IPR017821 Succinate CoA transferase
226 316 FunFam G3DSA:3.30.750.70:FF:000002 Acetyl-CoA hydrolase Ach1
13 215 Pfam PF02550 Acetyl-CoA hydrolase/transferase N-terminal domain
13 215 InterPro IPR003702 Acetyl-CoA hydrolase/transferase, N-terminal
336 476 Gene3D G3DSA:3.40.1080.20 -
336 476 InterPro IPR038460 Acetyl-CoA hydrolase/transferase, C-terminal domain superfamily
2 495 PANTHER PTHR43609 ACETYL-COA HYDROLASE
2 495 InterPro IPR046433 Acetyl-CoA hydrolase/transferase
10 178 Gene3D G3DSA:3.40.1080.10 -
6 176 FunFam G3DSA:3.40.1080.10:FF:000004 Acetyl-CoA hydrolase
228 318 Gene3D G3DSA:3.30.750.70 -
322 463 Pfam PF13336 Acetyl-CoA hydrolase/transferase C-terminal domain
322 463 InterPro IPR026888 Acetyl-CoA hydrolase/transferase C-terminal domain
3 222 SUPERFAMILY SSF100950 NagB/RpiA/CoA transferase-like
3 222 InterPro IPR037171 NagB/RpiA transferase-like

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

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 2G39
X-ray 2.10 Å A,B
100.0% 1-497
PDBe RCSB PDBj File
Viewing
AlphaFold PA5445
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 0.72
2 0.442

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 21.86 0.875
2 7.2 0.375
3 6.26 0.314
4 2.37 0.063
5 2.09 0.047

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.

53 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
0RQ
4EUC
B3EY95 791.5 Da LogP -1.23 TPSA 363.6 3 viol. ✓ Clean CC(=O)CCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O)…
0T1
5DW5
B3EY95 749.5 Da LogP -1.19 TPSA 346.6 3 viol. ✓ Clean CCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O)OP(=O)…
SPD
3GK7
Q9RM86 145.2 Da LogP -0.34 TPSA 64.1 ✓ Ro5 ✓ Clean C(CCNCCCN)CN

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.