KpATCC43816 Protein target profile

putative 2-dehydropantoate 2-reductase

Accession: VK055_1045

Gene: AIK79668.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GNZ5

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Length 296

Pocket druggability (P2Rank · AlphaFold DB model) 0.867

Metabolic reactions 2

Chokepoint Yes

Direct ligand evidence 0 51 total records

Functional annotation 1 EC 4 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

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

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 88.8% of genes in this genome. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Second pocket predictor agrees P2Rank predicted binding-site probability 0.87. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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: 0.7% 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: 96.25 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) 0.867

Structure A0A0H3GNZ5

Pocket Pocket 1

Druggability (FPocket) 0.301

Structure A0A0H3GNZ5

Pocket Pocket 4

ColabFold model

P2Rank 0.86 · Pocket 1

FPocket 0.07 · Pocket 22

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 35 / 4744 genomes with a hit

Prevalence 0.7%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Pantothenate and CoA biosynthesis, more central than 88.8% of genes in this genome, no human homolog detected.

Relative network centrality 88.8% more central than 88.8% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTAFPKVALIGPGAIGTTIAAALFERGRAPMVCGRTAHSALVLRTDEGEIVVPGPVYTDPMAIAAPFDLVFVAVKTTQTEAIAPWLTALCSPDTVVCVLQNGVEQRQQFAPLTGGATVLPSVVWFPAQRDADASVWLRAAPRLTLPDLPGAERVQQALAGTRCAVDLAADFTTVAWRKLLQNAVAGLMVLTGRRAGMFAREDITALGLAYLRECLQVARAEGAALSENVPEEIIAGFHRAPADLSTSILIDRLNGRPLEWDIRNGVVQRRGRQHGIPTPLSDIIVPLLAAASDGPG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

1.1.1.169

Gene Ontology (GO)

GO:0008677 Catalysis of the reaction: (R)-pantoate + NADP+ = 2-dehydropantoate + H+ + NADPH.
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:0015940 The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid. It is a B complex vitamin that is a constituent of coenzyme A and is distributed ubiquitously in foods.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
6	291	NCBIfam	TIGR00745	2-dehydropantoate 2-reductase
6	291	InterPro	IPR003710	Ketopantoate reductase ApbA/PanE
6	289	PANTHER	PTHR21708	PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
7	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
16	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
170	290	Pfam	PF08546	Ketopantoate reductase PanE/ApbA C terminal
170	290	InterPro	IPR013752	Ketopantoate reductase, C-terminal domain
170	296	Gene3D	G3DSA:1.10.1040.10	-
170	296	InterPro	IPR013328	6-phosphogluconate dehydrogenase, domain 2
21	296	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
2	169	Gene3D	G3DSA:3.40.50.720	-
6	131	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
6	131	InterPro	IPR036291	NAD(P)-binding domain superfamily
1	6	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
170	290	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
170	290	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
7	149	Pfam	PF02558	Ketopantoate reductase PanE/ApbA
7	149	InterPro	IPR013332	Ketopantoate reductase, N-terminal domain
7	24	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.

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

0.867

Likely same site as FPocket 4 1.6 Å 39 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.014

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #4

0.301 Unusual size

Likely same site as P2Rank 1 1.6 Å 39 shared residues 100% of smaller site

Show in viewer

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_A0A0H3GNZ5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1045	ColabFold	—	—	full sequence	—	Loaded

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.

51 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 1 records from similar proteins

Structural ligands 1 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AOT PDB via homolog 165.1 Da · LogP 0.71 · TPSA 66.4 Open detail RCSB PDB

ZINC1673043 ZINC proposed compound · Tanimoto 0.800 Detail ZINC

ZINC3274081 ZINC proposed compound · Tanimoto 0.762 Detail ZINC

ZINC15416969 ZINC proposed compound · Tanimoto 0.640 Detail ZINC

ZINC1751835 ZINC proposed compound · Tanimoto 0.640 Detail ZINC

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
AOT RCSB PDB	5X20	Q3Y316	165.1 Da LogP 0.71 TPSA 66.4	✓ Ro5	✓ Clean	`c1ccc(cc1)NC(=O)C(=O)O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC1673043 ZINC	0.800	240.3 Da LogP 2.26 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=O)Nc1ccccc1`
ZINC3274081 ZINC	0.762	402.4 Da LogP 2.84 TPSA 116.4	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=O)Nc1ccc(NC(=O)C(=O)Nc2ccccc2)…`
ZINC15416969 ZINC	0.640	244.0 Da LogP 1.47 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)C(=O)Nc1ccc(Br)cc1`
ZINC1751835 ZINC	0.640	225.2 Da LogP 2.51 TPSA 46.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=O)c1ccccc1`
ZINC12416741 ZINC	0.636	212.3 Da LogP 3.33 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)Nc1ccccc1`
ZINC3670768 ZINC	0.621	374.4 Da LogP 3.48 TPSA 95.5	✓ Ro5	✓ Clean	`O=C(O)C(=O)Nc1ccc(NC(=O)C(c2ccccc2)c2ccccc2)cc1`
ZINC1410200 ZINC	0.615	283.3 Da LogP 2.09 TPSA 90.8	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=NO)C(=O)Nc1ccccc1`
ZINC2961287 ZINC	0.615	258.3 Da LogP 2.40 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=O)Nc1ccc(F)cc1`
ZINC8737301 ZINC	0.615	254.3 Da LogP 2.57 TPSA 58.2	✓ Ro5	✓ Clean	`Cc1ccc(NC(=O)C(=O)Nc2ccccc2)cc1`
ZINC409026 ZINC	0.609	346.4 Da LogP 4.97 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)Nc1ccc(NC(=O)Nc2ccccc2)cc1`
ZINC3129966 ZINC	0.607	225.6 Da LogP 1.83 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)/C=C(\Cl)C(=O)Nc1ccccc1`
ZINC34870131 ZINC	0.607	209.2 Da LogP 0.41 TPSA 103.7	✓ Ro5	✓ Clean	`O=C(O)C(=O)Nc1cccc(C(=O)O)c1`
ZINC1682609 ZINC	0.593	207.2 Da LogP 0.91 TPSA 83.5	✓ Ro5	✓ Clean	`CC(=O)c1ccc(NC(=O)C(=O)O)cc1`
ZINC54829 ZINC	0.583	254.3 Da LogP 2.65 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CC(=O)Nc1ccccc1)Nc1ccccc1`
ZINC2165033 ZINC	0.577	201.2 Da LogP 1.11 TPSA 83.5	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)S(=O)(=O)O`
ZINC100030967 ZINC	0.571	205.2 Da LogP 1.17 TPSA 63.2	✓ Ro5	✓ Clean	`CC(=O)CC(=O)C(=O)Nc1ccccc1`
ZINC103594352 ZINC	0.571	211.6 Da LogP 2.65 TPSA 49.3	✓ Ro5	✓ Clean	`C/C(O)=C(\Cl)C(=O)Nc1ccccc1`
ZINC1203164 ZINC	0.571	358.4 Da LogP 3.73 TPSA 82.6	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=NNc1ccccc1)C(=O)Nc1ccccc1`
ZINC1689020 ZINC	0.571	342.4 Da LogP 4.35 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=Cc1ccccc1)C(=O)Nc1ccccc1`
ZINC20185080 ZINC	0.571	207.2 Da LogP 1.83 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)c1ccc(NC(=O)C(=O)O)cc1`
ZINC34267448 ZINC	0.571	221.2 Da LogP 1.06 TPSA 83.5	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)C(=O)Nc1ccccc1`
ZINC4702949 ZINC	0.571	206.2 Da LogP 1.15 TPSA 58.2	✓ Ro5	✓ Clean	`CC(C)NC(=O)C(=O)Nc1ccccc1`
ZINC1619310 ZINC	0.567	238.2 Da LogP 0.89 TPSA 104.7	✓ Ro5	✓ Clean	`COC(=O)Nc1cccc(NC(=O)C(=O)O)c1`
ZINC1697328 ZINC	0.563	300.3 Da LogP 2.32 TPSA 104.7	✓ Ro5	✓ Clean	`O=C(Nc1cccc(NC(=O)C(=O)O)c1)Oc1ccccc1`
ZINC20185146 ZINC	0.563	271.3 Da LogP 2.29 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(O)C(=O)Nc1ccc(OCc2ccccc2)cc1`
ZINC121422 ZINC	0.560	316.4 Da LogP 4.19 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)c1ccc(C(=O)Nc2ccccc2)cc1`
ZINC2507936 ZINC	0.560	268.3 Da LogP 3.04 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CCC(=O)Nc1ccccc1)Nc1ccccc1`
ZINC348926 ZINC	0.560	316.4 Da LogP 4.19 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)c1ccccc1C(=O)Nc1ccccc1`
ZINC100341550 ZINC	0.552	273.7 Da LogP 3.29 TPSA 53.5	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)/C(Cl)=N/Nc1ccccc1`
ZINC15909409 ZINC	0.552	241.2 Da LogP 1.66 TPSA 71.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=O)Nc1cccnc1`
ZINC20185140 ZINC	0.552	244.2 Da LogP -0.64 TPSA 126.6	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(NC(=O)C(=O)O)cc1`
ZINC228958230 ZINC	0.552	284.3 Da LogP 1.96 TPSA 95.5	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=O)Nc1ccccc1C(=O)O`
ZINC2901525 ZINC	0.552	208.2 Da LogP -0.27 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(NCCO)C(=O)Nc1ccccc1`
ZINC2994880 ZINC	0.552	204.2 Da LogP 0.90 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=O)NC1CC1`
ZINC3072899 ZINC	0.552	254.3 Da LogP 1.94 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(NCc1ccccc1)C(=O)Nc1ccccc1`
ZINC3190996 ZINC	0.552	207.2 Da LogP 1.58 TPSA 55.4	✓ Ro5	✓ Clean	`CC(C)OC(=O)C(=O)Nc1ccccc1`
ZINC3875722 ZINC	0.552	210.1 Da LogP 0.62 TPSA 109.5	✓ Ro5	✓ Clean	`O=C(O)C(=O)Nc1ccc([N+](=O)[O-])cc1`
ZINC8430974 ZINC	0.552	273.7 Da LogP 3.29 TPSA 53.5	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)/C(Cl)=N\Nc1ccccc1`
ZINC4312750 ZINC	0.548	233.1 Da LogP 1.73 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)C(=O)Nc1cccc(C(F)(F)F)c1`
ZINC17877797 ZINC	0.538	300.3 Da LogP 0.99 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)[C@@H](O)[C@@H](O)C(=O)Nc1ccccc1`
ZINC280744 ZINC	0.538	300.3 Da LogP 0.99 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)[C@@H](O)[C@H](O)C(=O)Nc1ccccc1`
ZINC280747 ZINC	0.538	300.3 Da LogP 0.99 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)[C@H](O)[C@@H](O)C(=O)Nc1ccccc1`
ZINC28416 ZINC	0.538	346.4 Da LogP 4.97 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)Nc1ccccc1NC(=O)Nc1ccccc1`
ZINC312939 ZINC	0.538	346.4 Da LogP 4.97 TPSA 82.3	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)Nc1cccc(NC(=O)Nc2ccccc2)c1`
ZINC108815643 ZINC	0.536	440.3 Da LogP 4.81 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)…`
ZINC2007905 ZINC	0.536	209.2 Da LogP 0.41 TPSA 103.7	✓ Ro5	✓ Clean	`O=C(O)C(=O)Nc1ccccc1C(=O)O`
ZINC100330964 ZINC	0.533	267.3 Da LogP 2.95 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)/C(O)=C/C(=O)c1ccccc1`
ZINC308538976 ZINC	0.533	206.2 Da LogP 2.18 TPSA 78.8	✓ Ro5	✓ Clean	`C/C(O)=C(\N=O)C(=O)Nc1ccccc1`
ZINC4839535 ZINC	0.533	257.3 Da LogP 1.81 TPSA 63.1	✓ Ro5	✓ Clean	`Cc1ccc(C)n1NC(=O)C(=O)Nc1ccccc1`
ZINC5042510 ZINC	0.533	241.2 Da LogP 1.66 TPSA 71.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)C(=O)Nc1ccccn1`

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.

Cross-references

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

Sequence

UniProt A0A0H3GNZ5

Pathways

BioCyc RXN-22913 KEGG R02472 BioCyc 2-DEHYDROPANTOATE-REDUCT-RXN