Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA2969
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2969 plsX
Status: annotated
Amino acids: 326
Structure source: AlphaFold

EC

2.3.1.274

GO

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0043811 Catalysis of the reaction: a fatty acyl-[acyl-carrier protein] + orthophosphate = acyl phosphate + [acyl-carrier protein]. GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. GO:0008654 The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester. GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor). GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
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 0.664

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MGGDFGPHCVVPASIAFLAENSSSQLILVGQPALLEELLSRYPSLDRQRLRVHAASEVIGSDERPSQALRGKPDASMRVALELVRDGRAHACVSAGNTGALMALSRHLLKTLPGIDRPAMVTAVPTEKGHCHLLDLGANVDCSAEHLYQFAVMGAVAAEALGCVSPRVALLNVGTEEIKGNQQVKLAASLLQKAQGLNFSGYIEGDGLYRGEADVVVCDGFVGNILLKASEGLAAMVSARIEQRFRDGLAAKLVGALALPLLRRLRGDIAPARYNGASFLGLQGIVVKSHGSAAEEGFQSALRRAALEVRENLPQRLHGRLEHLLL

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

2.3.1.274

Gene Ontology (GO)

6

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0043811 Catalysis of the reaction: a fatty acyl-[acyl-carrier protein] + orthophosphate = acyl phosphate + [acyl-carrier protein].
GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
GO:0008654 The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester.
GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Sequence Features

Domain/signature hits from InterPro and related databases.

12 records

Show feature table

Start	End	DB	Term	Name
1	324	Gene3D	G3DSA:3.40.718.10	Isopropylmalate Dehydrogenase
1	323	NCBIfam	TIGR00182	phosphate acyltransferase PlsX
1	323	InterPro	IPR012281	Phospholipid biosynthesis protein, PlsX-like
1	324	PANTHER	PTHR30100	FATTY ACID/PHOSPHOLIPID SYNTHESIS PROTEIN PLSX
1	324	InterPro	IPR012281	Phospholipid biosynthesis protein, PlsX-like
1	325	PIRSF	PIRSF002465	Phsphlp_syn_PlsX
1	325	InterPro	IPR012281	Phospholipid biosynthesis protein, PlsX-like
1	326	Hamap	MF_00019	Phosphate acyltransferase [plsX].
1	326	InterPro	IPR012281	Phospholipid biosynthesis protein, PlsX-like
1	315	Pfam	PF02504	Fatty acid synthesis protein
1	315	InterPro	IPR003664	Fatty acid synthesis PlsX protein
1	324	SUPERFAMILY	SSF53659	Isocitrate/Isopropylmalate dehydrogenase-like

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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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 PA2969	AlphaFold	—	—	full sequence	—	Viewing

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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				0.664
2				0.395

PA2969