Protein profile

KP13_25184

3-carboxy-cis,cis-muconate cycloisomerase

Genome: KpKP13

Gene: ANJ86612.1 pcaB Structure source: AlphaFold + ColabFold UniProt A0A0H3GSE2
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Amino acids 450
Annotations 5
Features 29
PDB binders 5
Druggability 0.55

Overview

Basic information about this protein and its source genome.

Accession
KP13_25184
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
ANJ86612.1 pcaB
Status
annotated
Amino acids
450
Structure source
AlphaFold + ColabFold
EC
5.5.1.2
GO
GO:0019619 The chemical reactions and pathways resulting in the breakdown of 3,4-dihydroxybenzoate. 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: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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
30.303
Human E-value
3.22e-10
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
96.61

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 0.55
Structure A0A0H3GSE2
Pocket Pocket 1
P2Rank 0.025
Structure A0A0H3GSE2
Pocket Pocket 1
ColabFold model
FPocket 0.57 · Pocket 1
P2Rank 0.053 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 31 / 4744 genomes with a hit
Normalized 0.007

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

4
  • GO:0019619 The chemical reactions and pathways resulting in the breakdown of 3,4-dihydroxybenzoate.
  • 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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

29 records
Show feature table
Start End DB Term Name
113 133 Coils Coil Coil
361 440 SMART SM00998 ADSL_C_2
361 440 InterPro IPR019468 Adenylosuccinate lyase C-terminal
273 289 PRINTS PR00145 Argininosuccinate lyase family signature
138 158 PRINTS PR00145 Argininosuccinate lyase family signature
97 119 PRINTS PR00145 Argininosuccinate lyase family signature
228 252 PRINTS PR00145 Argininosuccinate lyase family signature
3 442 CDD cd01597 pCLME
273 282 ProSitePatterns PS00163 Fumarate lyases signature.
273 282 InterPro IPR020557 Fumarate lyase, conserved site
9 445 PANTHER PTHR43172 ADENYLOSUCCINATE LYASE
360 447 Gene3D G3DSA:1.10.40.30 -
362 439 Pfam PF10397 Adenylosuccinate lyase C-terminus
362 439 InterPro IPR019468 Adenylosuccinate lyase C-terminal
1 359 Gene3D G3DSA:1.20.200.10 Fumarase/aspartase (Central domain)
143 161 PRINTS PR00149 Fumarate lyase superfamily signature
143 161 InterPro IPR000362 Fumarate lyase family
228 255 PRINTS PR00149 Fumarate lyase superfamily signature
228 255 InterPro IPR000362 Fumarate lyase family
273 289 PRINTS PR00149 Fumarate lyase superfamily signature
273 289 InterPro IPR000362 Fumarate lyase family
98 116 PRINTS PR00149 Fumarate lyase superfamily signature
98 116 InterPro IPR000362 Fumarate lyase family
9 446 SUPERFAMILY SSF48557 L-aspartase-like
9 446 InterPro IPR008948 L-Aspartase-like
10 345 NCBIfam TIGR02426 3-carboxy-cis,cis-muconate cycloisomerase
10 345 InterPro IPR012789 3-carboxy-cis,cis-muconate cycloisomerase-like
11 297 Pfam PF00206 Lyase
11 297 InterPro IPR022761 Fumarate lyase, N-terminal

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

Loading 3D structure...

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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_A0A0H3GSE2
AlphaFold — — full sequence — Viewing
ColabFold KP13_25184
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
4 0.072
9 0.072
2 0.009
28 0.0

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 1.72 0.025
2 1.69 0.024
3 1.32 0.013
4 1.18 0.009
5 1.07 0.006

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.