KpATCC43816 Protein target profile

aspartate 1-decarboxylase

Accession: VK055_2429

Gene: AIK81026.1 panD 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GRW9

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Length 126

Pocket druggability (FPocket · AlphaFold DB model) 0.234

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 60 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

Central metabolic position More central than 92.8% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. 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. Review the complete evidence below

Risks to review

Microbiome similarity 193 of 4744 screened genomes (4.1%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.23.

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: 4.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 55.319 Higher values support similarity to known essential genes.
DEG E-value: 1.6999999999999998e-30 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.6 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)

Structure A0A0H3GRW9

Pocket No pockets

Druggability (FPocket) 0.234

Structure A0A0H3GRW9

Pocket Pocket 4

ColabFold model

FPocket 0.134 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 193 / 4744 genomes with a hit

Prevalence 4.1%

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 92.8% of genes in this genome, no human homolog detected.

Relative network centrality 92.8% more central than 92.8% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MMRNMLQGKLHRVKVTQADLHYEGSCAIDQDFLDAAGILENETIHLWNVTNGNRFSTYAIAAERGSRIISVNGAAAHCASVGDILIIASFVTMSDEEARSWQPNIAYFEGDNEMKRQAKAIPVQVA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Unknown

Enzyme Commission (EC)

4.1.1.11

Gene Ontology (GO)

GO:0004068 Catalysis of the reaction: L-aspartate = beta-alanine + CO2.
GO:0006523 The chemical reactions and pathways resulting in the formation of alanine, 2-aminopropanoic acid.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

15 records

Show feature table

Start	End	DB	Term	Name
1	126	NCBIfam	TIGR00223	aspartate 1-decarboxylase
1	126	InterPro	IPR003190	Aspartate decarboxylase
1	125	PIRSF	PIRSF006246	ADC
1	125	InterPro	IPR003190	Aspartate decarboxylase
1	124	PANTHER	PTHR21012	ASPARTATE 1-DECARBOXYLASE
1	124	InterPro	IPR003190	Aspartate decarboxylase
1	126	FunFam	G3DSA:2.40.40.20:FF:000004	Aspartate 1-decarboxylase
1	126	Gene3D	G3DSA:2.40.40.20	-
1	126	Hamap	MF_00446	Aspartate 1-decarboxylase [panD].
2	112	CDD	cd06919	Asp_decarbox
2	112	InterPro	IPR003190	Aspartate decarboxylase
1	121	SUPERFAMILY	SSF50692	ADC-like
1	121	InterPro	IPR009010	Aspartate decarboxylase-like domain superfamily
1	114	Pfam	PF02261	Aspartate decarboxylase
1	114	InterPro	IPR003190	Aspartate decarboxylase

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 · FPocket

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

Pocket 1 FPocket #4

0.234

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:24-24 Schiff-base intermediate with substrate; via pyruvic acid

UniProt: Active site:57-57 Proton donor

UniProt: Binding site:56-56

UniProt: Binding site:72-74

Residue sets

UniProt: Active site:24-24 Schiff-base intermediate with substrate; via pyruvic acid

UniProt: Active site:57-57 Proton donor

UniProt: Binding site:56-56

UniProt: Binding site:72-74

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_A0A0H3GRW9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2429	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.

60 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

74C PDB via homolog 15.0 Da · LogP 0.45 · TPSA 0.0 Open detail RCSB PDB

CO2 PDB via homolog Detail RCSB PDB

FUM PDB via homolog Detail RCSB PDB

MLA PDB via homolog Detail RCSB PDB

MLI PDB via homolog Detail RCSB PDB

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
74C RCSB PDB	5LS7	P0A790	15.0 Da LogP 0.45 TPSA 0.0	✓ Ro5	✓ Clean	`[CH3]`
CO2 RCSB PDB	5LS7	P0A790	44.0 Da LogP -0.58 TPSA 34.1	✓ Ro5	✓ Clean	`C(=O)=O`
FUM RCSB PDB	2EEO	Q5SKN7	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
MLA RCSB PDB	1PQH	P0A790	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=O)O`
MLI RCSB PDB	4AZD	P0A790	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
NMJ RCSB PDB	6P02	P9WIL3	158.5 Da LogP 0.83 TPSA 63.1	✓ Ro5	✓ Clean	`c1c(nc(cn1)Cl)C(=O)O`
NSN RCSB PDB	1UHE	P56065	201.2 Da LogP -4.99 TPSA 140.3	✓ Ro5	✓ Clean	`CC(=[NH+][C@@H](CC(=O)[O-])C(=O)N)C(=O)N`
PYR RCSB PDB	6OYY	P9WIL3	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
TLA RCSB PDB	6P1Y	P9WIL3	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)O`
VGL RCSB PDB	6OYY	P9WIL3	124.1 Da LogP 0.17 TPSA 63.1	✓ Ro5	✓ Clean	`c1cnc(cn1)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
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC84307856 ZINC	0.593	203.0 Da LogP 0.94 TPSA 63.1	✓ Ro5	✓ Clean	`O=C(O)c1cncc(Br)n1`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC19092924 ZINC	0.581	211.7 Da LogP 1.37 TPSA 46.1	✓ Ro5	✓ Clean	`O=C(c1cncc(Cl)n1)N1CCCC1`
ZINC20357720 ZINC	0.581	228.2 Da LogP 1.41 TPSA 80.1	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1C(=O)c1cnccn1`
ZINC19092105 ZINC	0.563	225.7 Da LogP 1.76 TPSA 46.1	✓ Ro5	✓ Clean	`O=C(c1cncc(Cl)n1)N1CCCCC1`
ZINC211537376 ZINC	0.563	234.6 Da LogP 2.50 TPSA 63.1	✓ Ro5	✓ Clean	`O=C(O)c1cncc(-c2ccc(Cl)cc2)n1`
ZINC2749775 ZINC	0.552	272.3 Da LogP -0.57 TPSA 109.8	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)c1cnccn1)c1cnccn1`
ZINC20496347 ZINC	0.548	219.3 Da LogP 1.88 TPSA 46.1	✓ Ro5	✓ Clean	`O=C(c1cnccn1)N1CCCCCCC1`
ZINC5705248 ZINC	0.548	205.3 Da LogP 1.49 TPSA 46.1	✓ Ro5	✓ Clean	`O=C(c1cnccn1)N1CCCCCC1`
ZINC69048726 ZINC	0.548	201.2 Da LogP 1.24 TPSA 76.0	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2cnccn2)cn1`
ZINC12360654 ZINC	0.545	207.2 Da LogP 1.30 TPSA 76.0	✓ Ro5	✓ Clean	`O=C(O)c1csc(-c2cnccn2)n1`
ZINC26423456 ZINC	0.543	250.2 Da LogP 0.88 TPSA 105.1	✓ Ro5	✓ Clean	`O=C(O)c1csc(NC(=O)c2cnccn2)n1`
ZINC2580774 ZINC	0.531	216.3 Da LogP 2.41 TPSA 42.9	✓ Ro5	✓ Clean	`O=C(Sc1ccccc1)c1cnccn1`
ZINC19092635 ZINC	0.529	227.7 Da LogP 0.60 TPSA 55.3	✓ Ro5	✓ Clean	`O=C(c1cncc(Cl)n1)N1CCOCC1`
ZINC19092951 ZINC	0.529	240.7 Da LogP 0.52 TPSA 49.3	✓ Ro5	✓ Clean	`CN1CCN(C(=O)c2cncc(Cl)n2)CC1`
ZINC4749098 ZINC	0.529	243.2 Da LogP 1.43 TPSA 92.2	✓ Ro5	✓ Clean	`O=C(O)c1ccc(NC(=O)c2cnccn2)cc1`
ZINC71250791 ZINC	0.517	236.5 Da LogP 2.20 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1cc(Br)cc(Cl)n1`
ZINC238854040 ZINC	0.516	202.2 Da LogP -0.42 TPSA 97.2	✓ Ro5	✓ Clean	`CS(=O)(=O)c1cncc(C(=O)O)n1`
ZINC26423811 ZINC	0.516	200.2 Da LogP 1.84 TPSA 63.1	✓ Ro5	✓ Clean	`O=C(O)c1cncc(-c2ccccc2)n1`
ZINC2747329 ZINC	0.516	300.3 Da LogP 0.21 TPSA 109.8	✓ Ro5	✓ Clean	`O=C(NCCCCNC(=O)c1cnccn1)c1cnccn1`
ZINC2747452 ZINC	0.516	286.3 Da LogP -0.18 TPSA 109.8	✓ Ro5	✓ Clean	`O=C(NCCCNC(=O)c1cnccn1)c1cnccn1`
ZINC19092783 ZINC	0.515	205.2 Da LogP 0.28 TPSA 63.2	✓ Ro5	✓ Clean	`O=C1CCN(C(=O)c2cnccn2)CC1`
ZINC40542019 ZINC	0.515	209.3 Da LogP 0.67 TPSA 46.1	✓ Ro5	✓ Clean	`O=C(c1cnccn1)N1CCSCC1`
ZINC52508253 ZINC	0.515	201.6 Da LogP 0.76 TPSA 55.3	✓ Ro5	✓ Clean	`CON(C)C(=O)c1cncc(Cl)n1`
ZINC54792854 ZINC	0.515	202.2 Da LogP 0.63 TPSA 88.9	✓ Ro5	✓ Clean	`O=C(O)c1ccnc(-c2cnccn2)n1`
ZINC74212868 ZINC	0.515	201.2 Da LogP 1.24 TPSA 76.0	✓ Ro5	✓ Clean	`O=C(O)c1cccc(-c2cnccn2)n1`
ZINC79435988 ZINC	0.515	209.2 Da LogP -0.32 TPSA 83.4	✓ Ro5	✓ Clean	`CN(CC(=O)O)CC(=O)c1cnccn1`
ZINC96047318 ZINC	0.515	366.4 Da LogP 1.43 TPSA 92.2	✓ Ro5	✓ Clean	`O=C(c1cnccn1)N1CCC2(CC1)CCN(C(=O)c1cnccn1)CC2`
ZINC98181313 ZINC	0.515	268.1 Da LogP 3.04 TPSA 54.9	✓ Ro5	✓ Clean	`O=C(Nc1ccc(Cl)cc1)c1cncc(Cl)n1`
ZINC21953682 ZINC	0.514	235.2 Da LogP 0.41 TPSA 83.4	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)c2cnccn2)CC1`
ZINC138079998 ZINC	0.500	212.0 Da LogP 1.41 TPSA 37.3	✓ Ro5	✓ Clean	`C=C(I)CC(=O)O`
ZINC146844160 ZINC	0.500	237.4 Da LogP 1.59 TPSA 63.1	✓ Ro5	✓ Clean	`O=C(O)c1cnc(Cl)c(Br)n1`
ZINC20280834 ZINC	0.500	221.2 Da LogP 0.17 TPSA 83.4	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)c1cnccn1`
ZINC211537270 ZINC	0.500	234.6 Da LogP 2.50 TPSA 63.1	✓ Ro5	✓ Clean	`O=C(O)c1cncc(-c2cccc(Cl)c2)n1`
ZINC2755537 ZINC	0.500	328.4 Da LogP 0.99 TPSA 109.8	✓ Ro5	✓ Clean	`O=C(NCCCCCCNC(=O)c1cnccn1)c1cnccn1`
ZINC375500 ZINC	0.500	326.4 Da LogP 0.74 TPSA 109.8	✓ Ro5	✓ Clean	`O=C(NC1CCC(NC(=O)c2cnccn2)CC1)c1cnccn1`
ZINC37658100 ZINC	0.500	218.6 Da LogP 2.36 TPSA 42.9	✓ Ro5	✓ Clean	`O=C(c1ccc(Cl)cc1)c1cnccn1`
ZINC96053972 ZINC	0.500	324.3 Da LogP 0.11 TPSA 92.2	✓ Ro5	✓ Clean	`O=C(c1cnccn1)N1CC2CN(C(=O)c3cnccn3)CC2C1`
ZINC98181293 ZINC	0.500	247.7 Da LogP 2.06 TPSA 54.9	✓ Ro5	✓ Clean	`O=C(NCc1ccccc1)c1cncc(Cl)n1`
ZINC98181377 ZINC	0.500	302.5 Da LogP 3.69 TPSA 54.9	✓ Ro5	✓ Clean	`O=C(Nc1c(Cl)cccc1Cl)c1cncc(Cl)n1`

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 A0A0H3GRW9

Pathways

KEGG R00489 BioCyc ASPDECARBOX-RXN