Protein profile

KP13_01043

3-ketoacyl-CoA thiolase

Genome: KpKP13

Gene: fadI AHE43429.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GWF1
Export view
Amino acids 436
Annotations 9
Features 28
PDB binders 10
Druggability 0.76

Overview

Basic information about this protein and its source genome.

Accession
KP13_01043
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
fadI AHE43429.1
Status
annotated
Amino acids
436
Structure source
AlphaFold + ColabFold
EC
2.3.1.16
GO
GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor). GO:0016042 The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor). GO:0003988 Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
47.761
Human E-value
7.17e-59
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
95.72

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 0.76
Structure A0A0H3GWF1
Pocket Pocket 28
P2Rank 0.853
Structure A0A0H3GWF1
Pocket Pocket 1
ColabFold model
FPocket 0.792 · Pocket 26
P2Rank 0.85 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 123 / 4744 genomes with a hit
Normalized 0.026

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
  • GO:0016042 The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
  • GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
  • GO:0003988 Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0006635 A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).

Sequence Features

Domain/signature hits from InterPro and related databases.

28 records
Show feature table
Start End DB Term Name
15 295 SUPERFAMILY SSF53901 Thiolase-like
15 295 InterPro IPR016039 Thiolase-like
297 434 SUPERFAMILY SSF53901 Thiolase-like
297 434 InterPro IPR016039 Thiolase-like
8 435 Gene3D G3DSA:3.40.47.10 -
8 435 InterPro IPR016039 Thiolase-like
9 436 PIRSF PIRSF000429 Ac-CoA_Ac_transf
9 436 InterPro IPR002155 Thiolase
296 434 Pfam PF02803 Thiolase, C-terminal domain
296 434 InterPro IPR020617 Thiolase, C-terminal
417 430 ProSitePatterns PS00099 Thiolases active site.
417 430 InterPro IPR020610 Thiolase, active site
15 288 Pfam PF00108 Thiolase, N-terminal domain
15 288 InterPro IPR020616 Thiolase, N-terminal
17 434 NCBIfam TIGR01930 acetyl-CoA C-acyltransferase
17 434 InterPro IPR002155 Thiolase
382 398 ProSitePatterns PS00737 Thiolases signature 2.
382 398 InterPro IPR020613 Thiolase, conserved site
16 420 CDD cd00751 thiolase
16 420 InterPro IPR002155 Thiolase
7 435 FunFam G3DSA:3.40.47.10:FF:000011 3-ketoacyl-CoA thiolase
8 436 NCBIfam TIGR02446 acetyl-CoA C-acyltransferase FadI
8 436 InterPro IPR012806 Acetyl-CoA C-acyltransferase FadI
95 113 ProSitePatterns PS00098 Thiolases acyl-enzyme intermediate signature.
95 113 InterPro IPR020615 Thiolase, acyl-enzyme intermediate active site
12 435 PANTHER PTHR42689 ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED
2 436 Hamap MF_01618 3-ketoacyl-CoA thiolase [fadI].
2 436 InterPro IPR012806 Acetyl-CoA C-acyltransferase FadI

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

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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_A0A0H3GWF1
AlphaFold — — full sequence — Viewing
ColabFold KP13_01043
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
28 0.76

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 23.25 0.887
2 1.92 0.039

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

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
168
1OU6
P07097 388.5 Da LogP 0.15 TPSA 131.0 ✓ Ro5 ✓ Clean CC(=O)OCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COC(=O)C(C…
1VU
6BJB
F1KYX0 823.6 Da LogP -0.93 TPSA 363.6 3 viol. ✓ Clean CCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O…
5UG
5F38
P76461 438.3 Da LogP -0.85 TPSA 191.7 1 viol. ✓ Clean CC(C)(COP(=O)(O)OP(=O)(O)O)[C@@H](C(=O)NCCC(=O)…
CAA
1M1O
P07097 851.6 Da LogP -1.36 TPSA 380.7 3 viol. ✓ Clean CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…
COZ
5F38
P76461 767.5 Da LogP -1.67 TPSA 346.6 3 viol. ✓ Clean CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…
DNO
2WKU
P07097 180.2 Da LogP -3.38 TPSA 118.2 ✓ Ro5 ✓ Clean C([C@H]([C@H]([C@@H]([C@@H](C=O)O)O)O)O)O
DTT
4C2K
P42765 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CS)O)O)S
NH4
6ARE
Q4WCL5 18.0 Da LogP 0.38 TPSA 36.5 ✓ Ro5 ✓ Clean [NH4+]
OPI
2VU1
P07097 346.4 Da LogP -0.42 TPSA 125.0 ✓ Ro5 ✓ Clean CC(C)(C)C(=O)OCC(C)(C)[C@H](C(=O)NCCC(=O)NCCO)O
PN5
2VU2
P07097 362.5 Da LogP 0.52 TPSA 104.7 ✓ Ro5 ✓ Clean CC(C)(C)C(=O)OCC(C)(C)[C@H](C(=O)NCCC(=O)NCCS)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.