Protein profile

PA0230

3-carboxy-cis,cis-muconate cycloisomerase

Genome: NC_002516.2

Gene: PA0230 pcaB Structure source: AlphaFold UniProt Q9I6Q8
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Amino acids 459
Annotations 7
Features 32
PDB binders 5
Druggability 0.915

Overview

Basic information about this protein and its source genome.

Accession
PA0230
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA0230 pcaB
Status
annotated
Amino acids
459
Structure source
AlphaFold
EC
5.5.1.2
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0047472 Catalysis of the reaction: 2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate = 3-carboxy-cis,cis-muconate + H+. 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:0019619 The chemical reactions and pathways resulting in the breakdown of 3,4-dihydroxybenzoate. GO:0042952 A pathway of aromatic compound degradation by ortho-cleavage; one branch converts protocatechuate, derived from phenolic compounds, to beta-ketoadipate, and the other branch converts catechol, generated from various aromatic hydrocarbons, amino aromatics, and lignin monomers, also to beta-ketoadipate. Two additional steps accomplish the conversion of beta-ketoadipate to tricarboxylic acid cycle intermediates. 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
hit
Human identity (%)
31.443
Human E-value
1.12e-07
Gut microbiome off-target
hit
Essential (DEG)
N
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 0.915
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0047472 Catalysis of the reaction: 2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate = 3-carboxy-cis,cis-muconate + H+.
  • 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:0019619 The chemical reactions and pathways resulting in the breakdown of 3,4-dihydroxybenzoate.
  • GO:0042952 A pathway of aromatic compound degradation by ortho-cleavage; one branch converts protocatechuate, derived from phenolic compounds, to beta-ketoadipate, and the other branch converts catechol, generated from various aromatic hydrocarbons, amino aromatics, and lignin monomers, also to beta-ketoadipate. Two additional steps accomplish the conversion of beta-ketoadipate to tricarboxylic acid cycle intermediates.
  • 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.

32 records
Show feature table
Start End DB Term Name
9 449 SUPERFAMILY SSF48557 L-aspartase-like
9 449 InterPro IPR008948 L-Aspartase-like
342 362 Coils Coil Coil
367 448 FunFam G3DSA:1.10.40.30:FF:000007 Adenylosuccinate lyase
9 448 CDD cd01597 pCLME
3 366 Gene3D G3DSA:1.20.200.10 Fumarase/aspartase (Central domain)
2 364 FunFam G3DSA:1.20.200.10:FF:000014 3-carboxy-cis,cis-muconate cycloisomerase
279 288 ProSitePatterns PS00163 Fumarate lyases signature.
279 288 InterPro IPR020557 Fumarate lyase, conserved site
6 451 PANTHER PTHR43172 ADENYLOSUCCINATE LYASE
367 446 SMART SM00998 ADSL_C_2
367 446 InterPro IPR019468 Adenylosuccinate lyase C-terminal
367 453 Gene3D G3DSA:1.10.40.30 -
9 352 NCBIfam TIGR02426 3-carboxy-cis,cis-muconate cycloisomerase
9 352 InterPro IPR012789 3-carboxy-cis,cis-muconate cycloisomerase-like
368 445 Pfam PF10397 Adenylosuccinate lyase C-terminus
368 445 InterPro IPR019468 Adenylosuccinate lyase C-terminal
119 146 Coils Coil Coil
16 304 Pfam PF00206 Lyase
16 304 InterPro IPR022761 Fumarate lyase, N-terminal
104 122 PRINTS PR00149 Fumarate lyase superfamily signature
104 122 InterPro IPR000362 Fumarate lyase family
149 167 PRINTS PR00149 Fumarate lyase superfamily signature
149 167 InterPro IPR000362 Fumarate lyase family
234 261 PRINTS PR00149 Fumarate lyase superfamily signature
234 261 InterPro IPR000362 Fumarate lyase family
279 295 PRINTS PR00149 Fumarate lyase superfamily signature
279 295 InterPro IPR000362 Fumarate lyase family
234 258 PRINTS PR00145 Argininosuccinate lyase family signature
144 164 PRINTS PR00145 Argininosuccinate lyase family signature
103 125 PRINTS PR00145 Argininosuccinate lyase family signature
279 295 PRINTS PR00145 Argininosuccinate lyase family signature

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
AlphaFold PA0230
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
1 0.915
3 0.616
18 0.237

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.

55 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
DTT
1RE5
Q88N37 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CS)O)O)S
FUM
5XNZ
A0A0K2JL82 116.1 Da LogP -0.29 TPSA 74.6 ✓ Ro5 ✓ Clean C(=C/C(=O)O)\C(=O)O
MLI
2PFM
A0A6L8PR48 102.0 Da LogP -3.12 TPSA 80.3 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(=O)[O-]
OXL
2X75
Q7A0G9 88.0 Da LogP -3.51 TPSA 80.3 ✓ Ro5 ✓ Clean C(=O)(C(=O)[O-])[O-]
SIN
4EEI
Q5NIQ1 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean 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.