Protein profile

PA1580

citrate synthase

Genome: NC_002516.2

Gene: PA1580 gltA Structure source: Experimental + AlphaFold UniProt P14165
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Amino acids 428
Annotations 7
Features 34
PDB binders 3
Druggability 0.745

Overview

Basic information about this protein and its source genome.

Accession
PA1580
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1580 gltA
Status
annotated
Amino acids
428
Structure source
Experimental + AlphaFold
EC
2.3.3.16
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0036440 Catalysis of the reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA. GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0046912 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor), with the acyl group being converted into alkyl on transfer. GO:0004108 OBSOLETE. Catalysis of the reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA, where the acetyl group is added to the si-face of oxaloacetate; acetyl-CoA thus provides the two carbon atoms of the pro-S carboxymethyl group.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
26.343
Human E-value
6.64e-28
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 0.745
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MADKKAQLIIEGSAPVELPVLSGTMGPDVVDVRGLTATGHFTFDPGFMSTASCESKITYIDGDKGVLLHRGYPIEQLAEKSDYLETCYLLLNGELPTAAQKEQFVGTIKNHTMVHEQLKTFFNGFRRDAHPMAVMCGVIGALSAFYHDSLDINNPKHREVSAHRLIAKMPTIAAMVYKYSKGEPMMYPRNDLNYAENFLHMMFNTPCETKPISPVLAKAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIASGIAALWGPAHGGANEAVLRMLDEIGDVSNIDKFVEKAKDKNDPFKLMGFGHRVYKNFDPRAKVMKQTCDEVLQELGINDPQLELAMKLEEIARHDPYFVERNLYPNVDFYSGIILKAIGIPTSMFTVIFALARTVGWISHWQEMLSGPYKIGRPRQLYTGHTQRDFTALKDRG

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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0036440 Catalysis of the reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA.
  • GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0046912 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor), with the acyl group being converted into alkyl on transfer.
  • GO:0004108 OBSOLETE. Catalysis of the reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA, where the acetyl group is added to the si-face of oxaloacetate; acetyl-CoA thus provides the two carbon atoms of the pro-S carboxymethyl group.

Sequence Features

Domain/signature hits from InterPro and related databases.

34 records
Show feature table
Start End DB Term Name
37 428 PIRSF PIRSF001369 Citrate_synth
37 428 InterPro IPR024176 Citrate synthase, bacterial-type
60 409 Gene3D G3DSA:1.10.580.10 Citrate Synthase, domain 1
60 409 InterPro IPR016142 Citrate synthase-like, large alpha subdomain
388 428 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
364 387 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
379 393 PRINTS PR00143 Citrate synthase signature
379 393 InterPro IPR002020 Citrate synthase
165 178 PRINTS PR00143 Citrate synthase signature
165 178 InterPro IPR002020 Citrate synthase
219 234 PRINTS PR00143 Citrate synthase signature
219 234 InterPro IPR002020 Citrate synthase
241 269 PRINTS PR00143 Citrate synthase signature
241 269 InterPro IPR002020 Citrate synthase
296 316 PRINTS PR00143 Citrate synthase signature
296 316 InterPro IPR002020 Citrate synthase
359 375 PRINTS PR00143 Citrate synthase signature
359 375 InterPro IPR002020 Citrate synthase
15 421 NCBIfam TIGR01798 citrate synthase
15 421 InterPro IPR010953 Citrate synthase, type I
6 427 SUPERFAMILY SSF48256 Citrate synthase
6 427 InterPro IPR036969 Citrate synthase superfamily
268 376 FunFam G3DSA:1.10.230.10:FF:000002 Citrate synthase
303 315 ProSitePatterns PS00480 Citrate synthase signature.
303 315 InterPro IPR019810 Citrate synthase active site
46 410 Pfam PF00285 Citrate synthase, C-terminal domain
46 410 InterPro IPR002020 Citrate synthase
18 415 CDD cd06114 EcCS_like
18 415 InterPro IPR010953 Citrate synthase, type I
1 427 PANTHER PTHR42871 CITRATE SYNTHASE
268 376 Gene3D G3DSA:1.10.230.10 -
268 376 InterPro IPR016143 Citrate synthase-like, small alpha subdomain
1 363 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 50 Gene3D G3DSA:2.20.28.60 -

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 6ZU0
X-ray 3.40 Å A,B,C,D,E,F
100.0% 1-428
PDBe RCSB PDBj File
Viewing
AlphaFold PA1580
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 0.745

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 15.44 0.753
2 2.67 0.079
3 1.12 0.008

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.

40 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
CMC
4JAE
P0ABH7 825.6 Da LogP -1.78 TPSA 383.9 3 viol. ✓ Clean CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H](…
CMX
2H12
P20901 793.5 Da LogP -1.73 TPSA 383.9 3 viol. ✓ Clean CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H](…
OAA
4JAG
P0ABH7 131.1 Da LogP -2.22 TPSA 94.5 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)C(=O)[O-]

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.