Protein profile

KP13_04519

Catechol 1,2-dioxygenase

Genome: KpKP13

Gene: AHE44395.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GU08
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Amino acids 308
Annotations 10
Features 13
PDB binders 7
Druggability 0.131

Overview

Basic information about this protein and its source genome.

Accession
KP13_04519
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE44395.1
Status
annotated
Amino acids
308
Structure source
AlphaFold + ColabFold
EC
1.13.11.1
GO
GO:0016702 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from one donor, and two oxygen atoms is incorporated into a donor. GO:0009712 The chemical reactions and pathways involving a compound containing a pyrocatechol (1,2-benzenediol) nucleus or substituent. GO:0006725 OBSOLETE. The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells. GO:0018576 Catalysis of the reaction: catechol + O2 = cis,cis-muconate. GO:0019614 The chemical reactions and pathways resulting in the breakdown of catechol-containing compounds. Catechol is a compound containing a pyrocatechol nucleus or substituent. GO:0005506 Binding to an iron (Fe) ion.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
96.75

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 0.131
Structure A0A0H3GU08
Pocket Pocket 14
P2Rank 0.489
Structure A0A0H3GU08
Pocket Pocket 1
ColabFold model
FPocket 0.23 · Pocket 5
P2Rank 0.223 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 38 / 4744 genomes with a hit
Normalized 0.008

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • GO:0016702 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from one donor, and two oxygen atoms is incorporated into a donor.
  • GO:0009712 The chemical reactions and pathways involving a compound containing a pyrocatechol (1,2-benzenediol) nucleus or substituent.
  • GO:0006725 OBSOLETE. The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells.
  • GO:0018576 Catalysis of the reaction: catechol + O2 = cis,cis-muconate.
  • GO:0019614 The chemical reactions and pathways resulting in the breakdown of catechol-containing compounds. Catechol is a compound containing a pyrocatechol nucleus or substituent.
  • GO:0005506 Binding to an iron (Fe) ion.
  • 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:0008199 Binding to a ferric iron ion, Fe(III).
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

13 records
Show feature table
Start End DB Term Name
1 308 Gene3D G3DSA:2.60.130.10 Aromatic compound dioxygenase
1 308 InterPro IPR015889 Intradiol ring-cleavage dioxygenase, core
9 289 NCBIfam TIGR02439 catechol 1,2-dioxygenase
9 289 InterPro IPR012801 Catechol 1,2-dioxygenase, proteobacteria
8 291 SUPERFAMILY SSF49482 Aromatic compound dioxygenase
8 291 InterPro IPR015889 Intradiol ring-cleavage dioxygenase, core
27 95 Pfam PF04444 Catechol dioxygenase N terminus
27 95 InterPro IPR007535 Catechol dioxygenase, N-terminal
26 291 PANTHER PTHR33711 DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02910)-RELATED
135 163 ProSitePatterns PS00083 Intradiol ring-cleavage dioxygenases signature.
135 163 InterPro IPR000627 Intradiol ring-cleavage dioxygenase, C-terminal
105 289 Pfam PF00775 Dioxygenase
105 289 InterPro IPR000627 Intradiol ring-cleavage dioxygenase, C-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

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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_A0A0H3GU08
AlphaFold — — full sequence — Viewing
ColabFold KP13_04519
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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 7.39 0.387
2 2.2 0.053
3 1.76 0.032
4 1.26 0.012
5 1.0 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.

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
CAQ
1DLT
P07773 110.1 Da LogP 1.10 TPSA 40.5 ✓ Ro5 Alert c1ccc(c(c1)O)O
LIO
1DLM
P07773 636.9 Da LogP 8.51 TPSA 108.4 2 viol. ✓ Clean CCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+]…
MCT
1DMH
P07773 124.1 Da LogP 1.41 TPSA 40.5 ✓ Ro5 Alert Cc1ccc(c(c1)O)O
PCF
2AZQ
Q51433 734.1 Da LogP 10.61 TPSA 111.2 2 viol. ✓ Clean CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)([O-])OCC…
PG6
5UMH
A0A0H3KXJ8 266.3 Da LogP 0.35 TPSA 55.4 ✓ Ro5 ✓ Clean COCCOCCOCCOCCOCCOC
PIE
2XSV
Q9F103 836.1 Da LogP 7.65 TPSA 212.3 3 viol. ✓ Clean CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)([O-])OC1…
PTY
5TD3
A4JR51 734.1 Da LogP 11.67 TPSA 134.4 2 viol. ✓ Clean CCCCCCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCCCC…

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.