Protein profile

KP13_03551

Phosphoenolpyruvate-protein phosphotransferase

Genome: KpKP13

Gene: ptsI AHE43357.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3H186
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Amino acids 575
Annotations 9
Features 35
PDB binders 6
Druggability 0.63

Overview

Basic information about this protein and its source genome.

Accession
KP13_03551
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
ptsI AHE43357.1
Status
annotated
Amino acids
575
Structure source
AlphaFold + ColabFold
EC
2.7.3.9
GO
GO:0016310 The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor). 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:0009401 The uptake and phosphorylation of specific carbohydrates from the extracellular environment; uptake and phosphorylation are coupled, making the PTS a link between the uptake and metabolism of sugars; phosphoenolpyruvate is the original phosphate donor; phosphoenolpyruvate passes the phosphate via a signal transduction pathway, to enzyme 1 (E1), which in turn passes it on to the histidine protein, HPr; the next step in the system involves sugar-specific membrane-bound complex, enzyme 2 (EII), which transports the sugar into the cell; it includes the sugar permease, which catalyzes the transport reactions; EII is usually divided into three different domains, EIIA, EIIB, and EIIC. GO:0008965 Catalysis of the reaction: phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

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 (%)
50.351
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
90.25

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 0.63
Structure A0A0H3H186
Pocket Pocket 17
P2Rank 0.734
Structure A0A0H3H186
Pocket Pocket 1
ColabFold model
FPocket 0.404 · Pocket 36
P2Rank 0.592 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 261 / 4744 genomes with a hit
Normalized 0.055

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:0016310 The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
  • GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
  • 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:0009401 The uptake and phosphorylation of specific carbohydrates from the extracellular environment; uptake and phosphorylation are coupled, making the PTS a link between the uptake and metabolism of sugars; phosphoenolpyruvate is the original phosphate donor; phosphoenolpyruvate passes the phosphate via a signal transduction pathway, to enzyme 1 (E1), which in turn passes it on to the histidine protein, HPr; the next step in the system involves sugar-specific membrane-bound complex, enzyme 2 (EII), which transports the sugar into the cell; it includes the sugar permease, which catalyzes the transport reactions; EII is usually divided into three different domains, EIIA, EIIB, and EIIC.
  • GO:0008965 Catalysis of the reaction: phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
  • GO:0046872 Binding to a metal ion.

Sequence Features

Domain/signature hits from InterPro and related databases.

35 records
Show feature table
Start End DB Term Name
23 143 SUPERFAMILY SSF47831 Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain
23 143 InterPro IPR036618 PtsI, HPr-binding domain superfamily
138 235 FunFam G3DSA:3.50.30.10:FF:000001 Phosphoenolpyruvate-protein phosphotransferase
21 146 FunFam G3DSA:1.10.274.10:FF:000001 Phosphoenolpyruvate-protein phosphotransferase
232 259 Coils Coil Coil
21 146 Gene3D G3DSA:1.10.274.10 -
21 146 InterPro IPR036618 PtsI, HPr-binding domain superfamily
152 222 Pfam PF00391 PEP-utilising enzyme, mobile domain
152 222 InterPro IPR008279 PEP-utilising enzyme, mobile domain
250 541 Pfam PF02896 PEP-utilising enzyme, PEP-binding domain
250 541 InterPro IPR000121 PEP-utilising enzyme, C-terminal
396 419 Coils Coil Coil
2 566 NCBIfam TIGR01417 phosphoenolpyruvate--protein phosphotransferase
2 566 InterPro IPR006318 Phosphotransferase system, enzyme I-like
249 549 SUPERFAMILY SSF51621 Phosphoenolpyruvate/pyruvate domain
249 549 InterPro IPR015813 Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
125 246 SUPERFAMILY SSF52009 Phosphohistidine domain
125 246 InterPro IPR036637 Phosphohistidine domain superfamily
2 572 PANTHER PTHR46244 PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE
234 575 Gene3D G3DSA:3.20.20.60 -
234 575 InterPro IPR040442 Pyruvate kinase-like domain superfamily
447 465 ProSitePatterns PS00742 PEP-utilizing enzymes signature 2.
447 465 InterPro IPR023151 PEP-utilising enzyme, conserved site
4 126 Pfam PF05524 PEP-utilising enzyme, N-terminal
4 126 InterPro IPR008731 Phosphotransferase system, enzyme I N-terminal
184 195 ProSitePatterns PS00370 PEP-utilizing enzymes phosphorylation site signature.
184 195 InterPro IPR018274 PEP-utilising enzyme, active site
4 233 Gene3D G3DSA:3.50.30.10 Phosphohistidine domain
293 312 PRINTS PR01736 Phosphoenolpyruvate-protein phosphotransferase signature
500 512 PRINTS PR01736 Phosphoenolpyruvate-protein phosphotransferase signature
464 479 PRINTS PR01736 Phosphoenolpyruvate-protein phosphotransferase signature
447 462 PRINTS PR01736 Phosphoenolpyruvate-protein phosphotransferase signature
236 572 FunFam G3DSA:3.20.20.60:FF:000007 Phosphoenolpyruvate-protein phosphotransferase
1 574 PIRSF PIRSF000732 PTS_enzyme_I
1 574 InterPro IPR024692 Phosphotransferase system, enzyme I

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_A0A0H3H186
AlphaFold — — full sequence — Viewing
ColabFold KP13_03551
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
17 0.63

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 11.18 0.599
2 3.09 0.103
3 1.91 0.039
4 1.85 0.036
5 0.54 0.0

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.

56 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
6NQ
5JVL
P22221 569.1 Da LogP -0.65 TPSA 261.7 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
NH4
1KBL
P22983 18.0 Da LogP 0.38 TPSA 36.5 ✓ Ro5 ✓ Clean [NH4+]
OXL
2HWG
P08839 88.0 Da LogP -3.51 TPSA 80.3 ✓ Ro5 ✓ Clean C(=O)(C(=O)[O-])[O-]
PEP
1VBH
P11155 168.0 Da LogP -0.31 TPSA 104.1 ✓ Ro5 ✓ Clean C=C(C(=O)O)OP(=O)(O)O
PO3
2MP0
P08839 79.0 Da LogP -1.64 TPSA 63.2 ✓ Ro5 ✓ Clean [O-][P-](=O)[O-]
PPR
1KC7
P22983 168.0 Da LogP -1.18 TPSA 111.9 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)P(=O)(O)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.