Protein profile

PA0854

fumarate hydratase

Genome: NC_002516.2

Gene: fumC2 Structure source: ColabFold
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Amino acids 464
Annotations 6
Features 33
PDB binders 9
Druggability 0.691

Overview

Basic information about this protein and its source genome.

Accession
PA0854
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
fumC2
Status
annotated
Amino acids
464
Structure source
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:0004333 Catalysis of the reaction: (S)-malate = fumarate + H2O. 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:0045239 Any of the heteromeric enzymes that act in the TCA cycle. GO:0006106 The chemical reactions and pathways involving fumarate, the anion of trans-1,2-ethenedicarboxylic acid, the diastereoisomer of maleate. It is a key intermediate in metabolism and is formed in the TCA cycle from succinate and converted into malate.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
59.559
Human E-value
3.13e-48
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 0.691
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MSRTETDSLGTIEVPDDAYWGAQTQRSLENFAIGGQRMPLAVIHALALIKKAAARVNDHLGELPPEVARLIEQAADEVLAGRHDEHFPLVVWQTGSGTQTNMNVNEVIAGRANELAGNPRGGKSPVHPNDHVNRAQSSNDSFPTAMHIAAAKAVHEQLLPAIAELSGGLAEQSARHASLVKTGRTHLMDATPITFGQELSAFVAQLDYAERAIRAALPAVYQLAQGGTAVGTGLNAPKGFADAIAAEIAAESGLPFVAAPNKFAALAGHEPLVILSGALKSLAVALMKIANDLRLLGSGPRAGFAEVKLPANEPGSSIMPGKVNPTQCEALSMLACQVMGNDSTISFAASQGHLQLNVFKPVIVYNLLESIRLLADGCRNFNKHCVAGLEPDAQRMADLLERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLRAAALQLGYLDEAQFDEWVRPEQMLEAGHHG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • 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:0004333 Catalysis of the reaction: (S)-malate = fumarate + H2O.
  • 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:0045239 Any of the heteromeric enzymes that act in the TCA cycle.
  • GO:0006106 The chemical reactions and pathways involving fumarate, the anion of trans-1,2-ethenedicarboxylic acid, the diastereoisomer of maleate. It is a key intermediate in metabolism and is formed in the TCA cycle from succinate and converted into malate.

Sequence Features

Domain/signature hits from InterPro and related databases.

33 records
Show feature table
Start End DB Term Name
406 458 Pfam PF10415 Fumarase C C-terminus
406 458 InterPro IPR018951 Fumarase C, C-terminal
2 460 Hamap MF_00743 Fumarate hydratase class II [fumC].
2 460 InterPro IPR005677 Fumarate hydratase, class II
269 296 PRINTS PR00149 Fumarate lyase superfamily signature
269 296 InterPro IPR000362 Fumarate lyase family
178 196 PRINTS PR00149 Fumarate lyase superfamily signature
178 196 InterPro IPR000362 Fumarate lyase family
132 150 PRINTS PR00149 Fumarate lyase superfamily signature
132 150 InterPro IPR000362 Fumarate lyase family
315 331 PRINTS PR00149 Fumarate lyase superfamily signature
315 331 InterPro IPR000362 Fumarate lyase family
315 324 ProSitePatterns PS00163 Fumarate lyases signature.
315 324 InterPro IPR020557 Fumarate lyase, conserved site
10 340 Pfam PF00206 Lyase
10 340 InterPro IPR022761 Fumarate lyase, N-terminal
3 136 FunFam G3DSA:1.10.275.10:FF:000001 Fumarate hydratase, mitochondrial
3 136 Gene3D G3DSA:1.10.275.10 -
3 136 InterPro IPR024083 Fumarase/histidase, N-terminal
137 404 FunFam G3DSA:1.20.200.10:FF:000001 Fumarate hydratase, mitochondrial
137 403 Gene3D G3DSA:1.20.200.10 Fumarase/aspartase (Central domain)
3 459 SUPERFAMILY SSF48557 L-aspartase-like
3 459 InterPro IPR008948 L-Aspartase-like
3 457 CDD cd01362 Fumarase_classII
3 457 InterPro IPR005677 Fumarate hydratase, class II
173 193 PRINTS PR00145 Argininosuccinate lyase family signature
315 331 PRINTS PR00145 Argininosuccinate lyase family signature
131 153 PRINTS PR00145 Argininosuccinate lyase family signature
2 460 PANTHER PTHR11444 ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
3 458 NCBIfam TIGR00979 class II fumarate hydratase
3 458 InterPro IPR005677 Fumarate hydratase, class II
406 462 Gene3D G3DSA:1.10.40.30 -
405 461 FunFam G3DSA:1.10.40.30:FF:000002 Fumarate hydratase class II

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

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
ColabFold PA0854
ColabFold — — 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
1 0.691
2 0.222

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.

59 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
7C18
Q65UJ3 116.1 Da LogP -0.29 TPSA 74.6 ✓ Ro5 ✓ Clean C(=C/C(=O)O)\C(=O)O
LMR
6U4O
A0A3Q0KQY7 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
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.