Protein profile

KP13_00488

Aspartate ammonia-lyase

Genome: KpKP13

Gene: AHE46777.1 aspA Structure source: AlphaFold + ColabFold UniProt A0A0H3GM66
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Amino acids 478
Annotations 5
Features 30
PDB binders 8
Druggability 0.346

Overview

Basic information about this protein and its source genome.

Accession
KP13_00488
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE46777.1 aspA
Status
annotated
Amino acids
478
Structure source
AlphaFold + ColabFold
GO
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. 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:0008797 Catalysis of the reaction: L-aspartate = fumarate + NH4+.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
42.857
Human E-value
2.13e-27
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
77.612
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
95.73

Selected Druggability evidence

AlphaFold / UniProt model

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 0.346
Structure A0A0H3GM66
Pocket Pocket 1
P2Rank 0.071
Structure A0A0H3GM66
Pocket Pocket 1
ColabFold model
FPocket 0.236 · Pocket 5
P2Rank 0.094 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 580 / 4744 genomes with a hit
Normalized 0.122

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • 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.
  • 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:0008797 Catalysis of the reaction: L-aspartate = fumarate + NH4+.

Sequence Features

Domain/signature hits from InterPro and related databases.

30 records
Show feature table
Start End DB Term Name
6 458 CDD cd01357 Aspartase
137 159 PRINTS PR00145 Argininosuccinate lyase family signature
320 336 PRINTS PR00145 Argininosuccinate lyase family signature
178 198 PRINTS PR00145 Argininosuccinate lyase family signature
143 409 FunFam G3DSA:1.20.200.10:FF:000001 Fumarate hydratase, mitochondrial
320 329 ProSitePatterns PS00163 Fumarate lyases signature.
320 329 InterPro IPR020557 Fumarate lyase, conserved site
6 142 Gene3D G3DSA:1.10.275.10 -
6 142 InterPro IPR024083 Fumarase/histidase, N-terminal
320 336 PRINTS PR00149 Fumarate lyase superfamily signature
320 336 InterPro IPR000362 Fumarate lyase family
183 201 PRINTS PR00149 Fumarate lyase superfamily signature
183 201 InterPro IPR000362 Fumarate lyase family
138 156 PRINTS PR00149 Fumarate lyase superfamily signature
138 156 InterPro IPR000362 Fumarate lyase family
274 301 PRINTS PR00149 Fumarate lyase superfamily signature
274 301 InterPro IPR000362 Fumarate lyase family
1 458 SUPERFAMILY SSF48557 L-aspartase-like
1 458 InterPro IPR008948 L-Aspartase-like
6 474 NCBIfam TIGR00839 aspartate ammonia-lyase
6 474 InterPro IPR004708 Aspartate ammonia-lyase
143 410 Gene3D G3DSA:1.20.200.10 Fumarase/aspartase (Central domain)
411 464 Pfam PF10415 Fumarase C C-terminus
411 464 InterPro IPR018951 Fumarase C, C-terminal
13 345 Pfam PF00206 Lyase
13 345 InterPro IPR022761 Fumarate lyase, N-terminal
6 142 FunFam G3DSA:1.10.275.10:FF:000001 Fumarate hydratase, mitochondrial
411 460 FunFam G3DSA:1.10.40.30:FF:000003 Aspartate ammonia-lyase
411 459 Gene3D G3DSA:1.10.40.30 -
4 472 PANTHER PTHR42696 ASPARTATE AMMONIA-LYASE

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 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GM66
AlphaFold — — full sequence — Viewing
ColabFold KP13_00488
ColabFold — — 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 0.346

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 1.56 0.024
2 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.

58 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
APO
7LUB
P07954 169.1 Da LogP -1.42 TPSA 120.8 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)N)P(=O)(O)O
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
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
TLA
6VBE
P07954 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=O)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.