Protein profile

PA5429

aspartate ammonia-lyase

Genome: NC_002516.2

Gene: PA5429 aspA Structure source: AlphaFold UniProt Q9HTD7
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Amino acids 474
Annotations 8
Features 27
PDB binders 7
Druggability 0.78

Overview

Basic information about this protein and its source genome.

Accession
PA5429
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5429 aspA
Status
annotated
Amino acids
474
Structure source
AlphaFold
EC
4.3.1.1
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:0008797 Catalysis of the reaction: L-aspartate = fumarate + NH4+. GO:0045548 Catalysis of the reaction: L-phenylalanine = NH4 + trans-cinnamate. GO:0006531 The chemical reactions and pathways involving aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid. 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:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
42.317
Human E-value
1.54e-106
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 0.78
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0008797 Catalysis of the reaction: L-aspartate = fumarate + NH4+.
  • GO:0045548 Catalysis of the reaction: L-phenylalanine = NH4 + trans-cinnamate.
  • GO:0006531 The chemical reactions and pathways involving aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
  • 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:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
  • 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.

27 records
Show feature table
Start End DB Term Name
8 143 FunFam G3DSA:1.10.275.10:FF:000001 Fumarate hydratase, mitochondrial
322 331 ProSitePatterns PS00163 Fumarate lyases signature.
322 331 InterPro IPR020557 Fumarate lyase, conserved site
413 465 Pfam PF10415 Fumarase C C-terminus
413 465 InterPro IPR018951 Fumarase C, C-terminal
8 143 Gene3D G3DSA:1.10.275.10 -
8 143 InterPro IPR024083 Fumarase/histidase, N-terminal
8 467 NCBIfam TIGR00839 aspartate ammonia-lyase
8 467 InterPro IPR004708 Aspartate ammonia-lyase
144 411 FunFam G3DSA:1.20.200.10:FF:000001 Fumarate hydratase, mitochondrial
8 459 CDD cd01357 Aspartase
7 465 SUPERFAMILY SSF48557 L-aspartase-like
7 465 InterPro IPR008948 L-Aspartase-like
413 468 FunFam G3DSA:1.10.40.30:FF:000002 Fumarate hydratase class II
144 412 Gene3D G3DSA:1.20.200.10 Fumarase/aspartase (Central domain)
15 347 Pfam PF00206 Lyase
15 347 InterPro IPR022761 Fumarate lyase, N-terminal
7 470 PANTHER PTHR42696 ASPARTATE AMMONIA-LYASE
276 303 PRINTS PR00149 Fumarate lyase superfamily signature
276 303 InterPro IPR000362 Fumarate lyase family
184 202 PRINTS PR00149 Fumarate lyase superfamily signature
184 202 InterPro IPR000362 Fumarate lyase family
139 157 PRINTS PR00149 Fumarate lyase superfamily signature
139 157 InterPro IPR000362 Fumarate lyase family
322 338 PRINTS PR00149 Fumarate lyase superfamily signature
322 338 InterPro IPR000362 Fumarate lyase family
413 468 Gene3D G3DSA:1.10.40.30 -

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

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Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA5429
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
3 0.78
2 0.462

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.

57 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
FLC
6P3C
P05042 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
FUM
6WNG
A0A077EBQ3 116.1 Da LogP -0.29 TPSA 74.6 ✓ Ro5 ✓ Clean C(=C/C(=O)O)\C(=O)O
LMR
7C1A
Q65UJ3 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@@H](C(=O)O)O)C(=O)O
MLI
3GTD
Q9ZCQ4 102.0 Da LogP -3.12 TPSA 80.3 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(=O)[O-]
MLT
1FUO
P05042 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)O)C(=O)O
PMA
1FUP
P05042 254.1 Da LogP 0.48 TPSA 149.2 ✓ Ro5 ✓ Clean c1c(c(cc(c1C(=O)O)C(=O)O)C(=O)O)C(=O)O
SIF
1FUQ
P05042 190.3 Da LogP 1.25 TPSA 74.6 ✓ Ro5 ✓ Clean C[Si](C)(C)C(CC(=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.