KpATCC43816 Protein target profile

amidohydrolase family protein

Accession: VK055_3722

Gene: AIK82276.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A377U1J9
Length 304
Pocket druggability (P2Rank · AlphaFold DB model) 0.901
Direct ligand evidence 0 10 total records
Functional annotation 1 EC 5 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.

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
5.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

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

Structure confidence

ColabFold pLDDT
95.85 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) 0.901
Structure A0A377U1J9
Pocket Pocket 1
Druggability (FPocket) 0.862
Structure A0A377U1J9
Pocket Pocket 2
ColabFold model
P2Rank 0.907 · Pocket 1
FPocket 0.425 · Pocket 2
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 281 / 4744 genomes with a hit
Prevalence 5.9%

Metabolic context

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

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLEVKQEVAPWVELQIVAFPQEGILSYPNGEALLEEALKLGADVVGAIPHFEFTREYGVESLHIAFRLAQQYDRPLDIHCDEIDDEQSRFVETVAALALKAGIGPRVTASHTTAMHSYNGAYTSRLFRLLKLSGINFVANPLVNIHLQGRFDDYPKRRGITRVKELLAAGINVCFGHDDVFDPWYPLGTGNMLQVLHMGLHVCQLMGYQQINDGLQLITDNSARTFGLEDYGIVSGNPANLIILPAEDGFEAVRCQVPVRWSIRQGRVIATTQPAQSWIQTDRGGEELSFMRNSPLADAKGPKA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization
Cytoplasmic

Enzyme Commission (EC)

1

Gene Ontology (GO)

5
  • GO:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
  • GO:0004131 Catalysis of the reaction: cytosine + H2O = uracil + NH4+.
  • GO:0035888 Catalysis of the reaction: H+ + H2O + isoguanine = NH4+ + xanthine.
  • GO:0046872 Binding to a metal ion.
  • GO:0006209 The chemical reactions and pathways resulting in the breakdown of cytosine, 4-amino-2-hydroxypyrimidine, a pyrimidine derivative that is one of the five main bases found in nucleic acids; it occurs widely in cytidine derivatives.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

10 records
Show feature table
Start End DB Term Name
1 229 Gene3D G3DSA:3.20.20.140 -
1 240 SUPERFAMILY SSF51556 Metallo-dependent hydrolases
1 240 InterPro IPR032466 Metal-dependent hydrolase
1 269 CDD cd01293 Bact_CD
1 230 FunFam G3DSA:3.20.20.140:FF:000019 Cytosine deaminase
230 276 Gene3D G3DSA:2.30.40.10 Urease, subunit C, domain 1
230 276 InterPro IPR011059 Metal-dependent hydrolase, composite domain superfamily
1 279 PANTHER PTHR32027 CYTOSINE DEAMINASE
16 269 Pfam PF07969 Amidohydrolase family
16 269 InterPro IPR013108 Amidohydrolase 3

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
0.901
Likely same site as FPocket 2 2.7 Å 37 shared residues 97% of smaller site
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Surrounding area
Pocket 2 P2Rank #2
0.772
Show in viewer
Surrounding area
Pocket 3 P2Rank #3
0.073
Show in viewer
Surrounding area
Pocket 4 P2Rank #4
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 #2
0.862 Unusual size
Likely same site as P2Rank 1 2.7 Å 37 shared residues 97% 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_A0A377U1J9
AlphaFold DB full sequence Viewing
ColabFold VK055_3722
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.

10 records
Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records
Transferred evidence 6 records from similar proteins
Structural ligands 6 0 loaded crystals
Measured bioactivity 0 direct and transferred ChEMBL records
Proposed compounds 4 similarity-based ZINC candidates
Best available ligand signal
FPY PDB via homolog 132.1 Da · LogP -0.57 · TPSA 61.4 Open detail RCSB PDB
HPY PDB via homolog Detail RCSB PDB
IGA PDB via homolog Detail RCSB PDB
MLI PDB via homolog Detail RCSB PDB
O7U PDB via homolog Detail RCSB PDB

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
FPY RCSB PDB P25524 132.1 Da LogP -0.57 TPSA 61.4 ✓ Ro5 ✓ Clean C1=C([C@@H](NC(=O)N1)O)F
HPY RCSB PDB P25524 114.1 Da LogP -0.87 TPSA 61.4 ✓ Ro5 ✓ Clean C1=CNC(=O)N[C@H]1O
IGA RCSB PDB P25524 151.1 Da LogP -0.77 TPSA 100.5 ✓ Ro5 ✓ Clean c1[nH]c2c(n1)NC(=O)N=C2N
MLI RCSB PDB O52063 102.0 Da LogP -3.12 TPSA 80.3 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(=O)[O-]
O7U RCSB PDB P25524 147.1 Da LogP -0.08 TPSA 84.2 ✓ Ro5 ✓ Clean C1=C[P@](=O)(NC(=O)N1)N
PXN RCSB PDB P25524 368.5 Da LogP -0.44 TPSA 117.8 ✓ Ro5 ✓ Clean C[C@H](COCC(COC[C@@H](C)O)(COC[C@@H](C)O)COC[C@…

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.