KpKP13 Protein target profile

epoxyqueosine reductase

Accession: KP13_00524

Gene: AHE46742.1 queG 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GM97
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Length 379
Pocket druggability (P2Rank · AlphaFold DB model) 0.969
Functional annotation 1 EC 8 GO
Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. Structure available AlphaFold DB model + ColabFold model

Risks to review

Microbiome similarity 153 of 4744 screened genomes (3.2%) have a significant similarity hit. This target also has a predicted binding pocket (P2Rank 0.97) — check the ligand evidence before deprioritizing on off-target risk alone. Weak predicted binding pocket FPocket selected-pocket score 0.28.

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein. No ligand evidence No experimental PDB ligands, measured ChEMBL bioactivity, or proposed ZINC compound records are available.
Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target
No hit
Gut microbiome similarity
3.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
N
DEG identity (%)
0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT
94.54 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.969
Structure A0A0H3GM97
Pocket Pocket 1
Druggability (FPocket) 0.283
Structure A0A0H3GM97
Pocket Pocket 18
ColabFold model
P2Rank 0.967 · Pocket 1
FPocket 0.604 · Pocket 20
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 153 / 4744 genomes with a hit
Prevalence 3.2%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GM97

Sequence

Primary amino-acid sequence viewer.

MSQPLDLVQLAQQIKQWGTELGFQQVGIADTDLSASEPKLQAWLDKQYHGEMEWMARHGMMRARPHELLPGTLRVISVRMNYLPANAAFARTLKDPTLGYVSRYALGRDYHKLLRNRLKKLGEKIQEQCASLNFRPFVDSAPILERPIAEKAGLGWTGKHSLILSRDAGSFFFLGELLIDLPLPVDSPVAEECGRCVACMTICPTGAIVEPYTVDARRCISYLTIELEGAIPEEFRPLIGNRIYGCDDCQLICPWNRFSQLTDEEDFSPRKALHAPPLVELFAWSEAWFLKVTEGSAIRRIGHLRWLRNIAVALGNAPWDEAHLRALESRRGEHPLLDEHIEWAIAQQLKKRNADAVEVQLPKKLRLVRVVEKGLPRDA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization
Cytoplasmic

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0008033 The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.
  • GO:0008616 The chemical reactions and pathways resulting in the formation of queuosines, a series of nucleosides found in position 34 of tRNA and having an additional pentenyl ring added via an NH group to the methyl group of 7-methylguanosine. The pentenyl ring may carry other substituents. The wobble nucleoside of the tRNA sequence (position 34) corresponds to the first position of the anticodon.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
  • GO:0031419 Binding to cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
  • GO:0052693 Catalysis of the reaction: epoxyqueuosine in tRNA + reductant = queuosine in tRNA + oxidised reductant.
  • GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

16 records
Show feature table
Start End DB Term Name
193 256 Pfam PF13484 4Fe-4S double cluster binding domain
14 348 NCBIfam TIGR00276 tRNA epoxyqueuosine(34) reductase QueG
14 348 InterPro IPR004453 Epoxyqueuosine reductase QueG
139 256 SUPERFAMILY SSF46548 alpha-helical ferredoxin
7 315 Hamap MF_00916 Epoxyqueuosine reductase [queG].
7 315 InterPro IPR004453 Epoxyqueuosine reductase QueG
193 204 ProSitePatterns PS00198 4Fe-4S ferredoxin-type iron-sulfur binding region signature.
193 204 InterPro IPR017900 4Fe-4S ferredoxin, iron-sulphur binding, conserved site
62 140 Pfam PF08331 Epoxyqueuosine reductase QueG, DUF1730
62 140 InterPro IPR013542 Epoxyqueuosine reductase QueG, DUF1730
181 213 ProSiteProfiles PS51379 4Fe-4S ferredoxin-type iron-sulfur binding domain profile.
181 213 InterPro IPR017896 4Fe-4S ferredoxin-type, iron-sulphur binding domain
188 258 Gene3D G3DSA:3.30.70.20 -
5 346 PANTHER PTHR30002 EPOXYQUEUOSINE REDUCTASE
5 346 InterPro IPR004453 Epoxyqueuosine reductase QueG
188 258 FunFam G3DSA:3.30.70.20:FF:000017 Epoxyqueuosine reductase

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low
How colors and pocket overlays are used
Uniform protein color marks the displayed model as a single molecular object.
Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.
Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.
'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.
'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.
'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.
Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1
0.969
Likely same site as FPocket 18 7.8 Å 21 shared residues 68% of smaller site
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Surrounding area
Pocket 2 P2Rank #2
0.085
Show in viewer
Surrounding area
Pocket 3 P2Rank #3
0.003
Show in viewer
Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #18
0.283 Unusual size
Likely same site as P2Rank 1 7.8 Å 21 shared residues 68% of smaller site
Show in viewer
Surrounding area
Residue sets
UniProt: Active site:139-139 Proton donor
UniProt: Binding site:139-139
UniProt: Binding site:157-157
UniProt: Binding site:163-163
UniProt: Binding site:174-174
UniProt: Binding site:193-193
UniProt: Binding site:196-196
UniProt: Binding site:199-199
UniProt: Binding site:203-203
UniProt: Binding site:219-219
UniProt: Binding site:221-221
UniProt: Binding site:246-246
UniProt: Binding site:246-247
UniProt: Binding site:249-249
UniProt: Binding site:253-253
UniProt: Binding site:62-62
All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold DB AF_A0A0H3GM97
AlphaFold DB — — full sequence — Viewing
ColabFold KP13_00524
ColabFold — — full sequence — Loaded