Protein target profile

KP13_02142

Gamma-glutamyl phosphate reductase

Genome: KpKP13 Gene: AHE46148.1 proA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GNT9
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Length 417
Pocket druggability 0.172
Functional annotation 1 EC 7 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.53. Structure available AlphaFold DB model + ColabFold model

Risks to review

Human similarity Top human hit identity: 36.211%. Microbiome similarity 187 of 4744 screened genomes (3.9%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.17.

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
Hit
Human identity (%)
36.211 Lower values reduce human off-target concern.
Human E-value
2.64e-82
Gut microbiome similarity
3.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
Y
DEG identity (%)
50.529 Higher values support similarity to known essential genes.
DEG E-value
3.34e-130 Smaller values mean stronger essential-gene similarity.

Localization

Localization
Cytoplasmic

Structure confidence

ColabFold pLDDT
95.86 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.172
Structure A0A0H3GNT9
Pocket Pocket 3
P2Rank 0.529
Structure A0A0H3GNT9
Pocket Pocket 1
ColabFold model
FPocket 0.163 · Pocket 3
P2Rank 0.482 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 187 / 4744 genomes with a hit
Prevalence 3.9%

Cross-references

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

Sequence

UniProt A0A0H3GNT9

Sequence

Primary amino-acid sequence viewer.

MLEKMGIAAKAASWQLALLSSREKNQVLEKIADYLEAQTDDILRANAEDLAEARANGLSEAMLDRLALTPARLSGIASDVRQVCNLADPVGQVIDGGLLDSGLRIERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAAILRGGKETWRTNAATVKVIQQALQECGLPAAAVQAIESPDRALVGEMLKMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIFVDETAEIAPALKIIVNAKTQRPSTCNTVETLLVHRNIADTFLPALSKQMAESGVTLHAAPSALPALQNGPAKVEPVKAEQYDDEYLSLDLNVKVVADMDEAIAHIREHGTQHSDAILTRTLRNANRFINEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTTYKWIGFGDDTIRA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • GO:0006561 OBSOLETE. The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
  • 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:0004350 Catalysis of the reaction: L-glutamate 5-semialdehyde + NADP+ + phosphate = L-glutamyl 5-phosphate + H+ + NADPH.
  • GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
  • GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0055129 The chemical reactions and pathways resulting in the formation of L-proline, an L-enantiomer of a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records
Show feature table
Start End DB Term Name
11 413 Gene3D G3DSA:3.40.605.10 Aldehyde Dehydrogenase; Chain A, domain 1
11 413 InterPro IPR016162 Aldehyde dehydrogenase, N-terminal
9 406 NCBIfam TIGR00407 glutamate-5-semialdehyde dehydrogenase
9 406 InterPro IPR000965 GPR domain
1 417 PIRSF PIRSF000151 GPR
1 417 InterPro IPR012134 Glutamate-5-semialdehyde dehydrogenase
222 374 Gene3D G3DSA:3.40.309.10 Aldehyde Dehydrogenase; Chain A, domain 2
222 374 InterPro IPR016163 Aldehyde dehydrogenase, C-terminal
323 344 ProSitePatterns PS01223 Gamma-glutamyl phosphate reductase signature.
323 344 InterPro IPR020593 Gamma-glutamyl phosphate reductase GPR, conserved site
3 416 PANTHER PTHR11063 GLUTAMATE SEMIALDEHYDE DEHYDROGENASE
222 374 FunFam G3DSA:3.40.309.10:FF:000006 Gamma-glutamyl phosphate reductase
3 412 CDD cd07079 ALDH_F18-19_ProA-GPR
3 412 InterPro IPR000965 GPR domain
8 280 Pfam PF00171 Aldehyde dehydrogenase family
8 280 InterPro IPR015590 Aldehyde dehydrogenase domain
3 415 SUPERFAMILY SSF53720 ALDH-like
3 415 InterPro IPR016161 Aldehyde/histidinol dehydrogenase
1 416 Hamap MF_00412 Gamma-glutamyl phosphate reductase [proA].
1 416 InterPro IPR000965 GPR domain

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

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1
0.529
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Surrounding area
Site 2 P2Rank #2
0.029
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Surrounding area
Site 3 P2Rank #3
0.013
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Surrounding area
Site 4 P2Rank #4
0.007
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Surrounding area
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_A0A0H3GNT9
AlphaFold DB — — full sequence — Viewing
ColabFold KP13_02142
ColabFold — — full sequence — Loaded