Protein profile

KP13_31940

Formate acetyltransferase

Genome: KpKP13

Gene: AHE43941.1 pfl Structure source: AlphaFold + ColabFold UniProt A0A0J2FYK2
Amino acids 764
Annotations 7
Features 19
PDB binders 8
Druggability 0.536

Overview

Basic information about this protein and its source genome.

Accession
KP13_31940
Gene
AHE43941.1 pfl
Status
annotated
Amino acids
764
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
74.605
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
97.14

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.536
Structure A0A0J2FYK2
Pocket Pocket 36
P2Rank 0.317
Structure A0A0J2FYK2
Pocket Pocket 1
ColabFold model
FPocket 0.349 · Pocket 4
P2Rank 0.535 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 2502 / 4744 genomes with a hit
Normalized 0.527

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0008861 Catalysis of the reaction: acetyl-CoA + formate = CoA + pyruvate.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0006006 The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records
Show feature table
Start End DB Term Name
9 763 PANTHER PTHR30191 FORMATE ACETYLTRANSFERASE
15 764 NCBIfam TIGR01255 formate C-acetyltransferase
15 764 InterPro IPR005949 Formate acetyltransferase
7 764 FunFam G3DSA:3.20.70.20:FF:000003 Formate acetyltransferase
12 764 PIRSF PIRSF000379 For_Ac_trans_1
634 745 Pfam PF01228 Glycine radical
634 745 InterPro IPR001150 Glycine radical domain
7 764 Gene3D G3DSA:3.20.70.20 -
27 618 Pfam PF02901 Pyruvate formate lyase-like
27 618 InterPro IPR004184 Pyruvate formate lyase domain
734 742 ProSitePatterns PS00850 Glycine radical domain signature.
734 742 InterPro IPR019777 Formate C-acetyltransferase glycine radical, conserved site
15 760 CDD cd01678 PFL1
15 760 InterPro IPR005949 Formate acetyltransferase
636 764 ProSiteProfiles PS51149 Glycine radical domain profile.
636 764 InterPro IPR001150 Glycine radical domain
8 629 ProSiteProfiles PS51554 Pyruvate formate-lyase domain profile.
8 629 InterPro IPR004184 Pyruvate formate lyase domain
8 762 SUPERFAMILY SSF51998 PFL-like glycyl radical enzymes

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

Loading 3D structure...

Legend High Medium Low

Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0J2FYK2
AlphaFold full sequence Viewing
ColabFold KP13_31940
ColabFold full sequence Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
36 0.536
4 0.242
31 0.237

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 4.03 0.161
2 3.01 0.099
3 2.54 0.072
4 1.51 0.022
5 1.38 0.017

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.

28 records

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
8X3 E5Y378 126.1 Da LogP -1.13 TPSA 74.6 ✓ Ro5 ✓ Clean C(CS(=O)(=O)O)O
BTL Q30W70 102.2 Da LogP -0.11 TPSA 17.1 ✓ Ro5 ✓ Clean C[N+](C)(C)CC=O
CHT A0A0M3KL44 104.2 Da LogP -0.32 TPSA 20.2 ✓ Ro5 ✓ Clean C[N+](C)(C)CCO
DTL P09373 122.1 Da LogP -2.31 TPSA 80.9 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CO)O)O)O
HYP A0A031WDE4 131.1 Da LogP -1.21 TPSA 69.6 ✓ Ro5 ✓ Clean C1[C@H](CN[C@@H]1C(=O)O)O
MLI Q30W70 102.0 Da LogP -3.12 TPSA 80.3 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(=O)[O-]
PYR P09373 88.1 Da LogP -0.34 TPSA 54.4 ✓ Ro5 ✓ Clean CC(=O)C(=O)O
RP7 Q30W70 113.2 Da LogP -0.15 TPSA 23.5 ✓ Ro5 ✓ Clean CN1CC=C[C@@H](C1)O

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.