Protein profile

PA0337

phosphoenolpyruvate-protein phosphotransferase PtsP

Genome: NC_002516.2

Gene: ptsP PA0337 Structure source: AlphaFold UniProt G3XD36
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Amino acids 759
Annotations 11
Features 33
PDB binders 5
Druggability 0.729

Overview

Basic information about this protein and its source genome.

Accession
PA0337
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
ptsP PA0337
Status
annotated
Amino acids
759
Structure source
AlphaFold
EC
2.7.3.9
GO
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. GO:0008965 Catalysis of the reaction: phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine. GO:0015764 The directed movement of N-acetylglucosamine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Selected Druggability evidence

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 0.729
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MLNTLRKIVQEVNSAKDLKAALGIIVQRVKEAMGTQVCSVYLLDTETQRFVLMATEGLNKRSIGKVSMAPSEGLVGLVGTREEPLNLENAAAHPRYRYFAETGEERYASFLGAPIIHHRRVMGVLVVQQKERRQFDEGEEAFLVTMSAQLAGVIAHAEATGSIRGLGKLGKGIQEAKFVGVPGAPGVGVGKAVVVLPPADLEVVPDKQVDDIDAEIALFKQALEGVRADMRALSSKLASQLRKEERALFDVYLMMLDDASIGNEVKRIIRTGQWAQGALRQVVMEHVQRFELMDDAYLRERASDVKDIGRRLLAYLQEERKQNLTYPEQTIIVSEELSPAMLGEVPEGRLVGLVSVLGSGNSHVAILARAMGIPTVMGAVDLPYSKVDGIDLIVDGYHGEVYTNPSAELVRQYSDVVAEERELSKGLAALRELPCETLDGHRMPLWVNTGLLADVARAQERGAEGVGLYRTEVPFMINDRFPSEKEQLAIYREQLSAFHPLPVTMRTLDIGGDKALSYFPIKEDNPFLGWRGIRVTLDHPEIFLVQTRAMLKASEGLDNLRILLPMISGTHELEEALHLIHRAWGEVRDEGVDIAMPPIGMMVEIPAAVYQTRELARQVDFLSVGSNDLTQYLLAVDRNNPRVADLYDYLHPAVLHALKKVVDDAHLEGKPVSICGEMAGDPAAAVLLMAMGFDSLSMNATNLPKVKWLLRQITLDKARDLLGQLLTFDNPQVIHSSLHLALRNLGLGRVINPAATVQP

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

10
  • 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.
  • GO:0008965 Catalysis of the reaction: phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.
  • GO:0015764 The directed movement of N-acetylglucosamine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • 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: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:0005515 Binding to a protein.
  • GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

33 records
Show feature table
Start End DB Term Name
1 163 Gene3D G3DSA:3.30.450.40 -
1 163 InterPro IPR029016 GAF-like domain superfamily
327 399 Pfam PF00391 PEP-utilising enzyme, mobile domain
327 399 InterPro IPR008279 PEP-utilising enzyme, mobile domain
180 301 Pfam PF05524 PEP-utilising enzyme, N-terminal
180 301 InterPro IPR008731 Phosphotransferase system, enzyme I N-terminal
179 736 NCBIfam TIGR01417 phosphoenolpyruvate--protein phosphotransferase
179 736 InterPro IPR006318 Phosphotransferase system, enzyme I-like
204 316 SUPERFAMILY SSF47831 Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain
204 316 InterPro IPR036618 PtsI, HPr-binding domain superfamily
427 715 SUPERFAMILY SSF51621 Phosphoenolpyruvate/pyruvate domain
427 715 InterPro IPR015813 Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
620 638 ProSitePatterns PS00742 PEP-utilizing enzymes signature 2.
620 638 InterPro IPR023151 PEP-utilising enzyme, conserved site
17 164 SMART SM00065 gaf_1
17 164 InterPro IPR003018 GAF domain
620 635 PRINTS PR01736 Phosphoenolpyruvate-protein phosphotransferase signature
673 685 PRINTS PR01736 Phosphoenolpyruvate-protein phosphotransferase signature
467 486 PRINTS PR01736 Phosphoenolpyruvate-protein phosphotransferase signature
637 652 PRINTS PR01736 Phosphoenolpyruvate-protein phosphotransferase signature
17 152 Pfam PF01590 GAF domain
17 152 InterPro IPR003018 GAF domain
180 407 Gene3D G3DSA:3.50.30.10 Phosphohistidine domain
198 321 Gene3D G3DSA:1.10.274.10 -
198 321 InterPro IPR036618 PtsI, HPr-binding domain superfamily
81 740 PANTHER PTHR46244 PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE
300 420 SUPERFAMILY SSF52009 Phosphohistidine domain
300 420 InterPro IPR036637 Phosphohistidine domain superfamily
426 713 Pfam PF02896 PEP-utilising enzyme, PEP-binding domain
426 713 InterPro IPR000121 PEP-utilising enzyme, C-terminal
408 745 Gene3D G3DSA:3.20.20.60 -
408 745 InterPro IPR040442 Pyruvate kinase-like domain superfamily
2 158 SUPERFAMILY SSF55781 GAF domain-like

3D Structure

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

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Structural evidence

0 + 1

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA0337
AlphaFold — — full sequence — Viewing
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
1 0.267

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.

55 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)…
OXL
2HWG
P08839 88.0 Da LogP -3.51 TPSA 80.3 ✓ Ro5 ✓ Clean C(=O)(C(=O)[O-])[O-]
P4G
3CI6
Q6FEW8 162.2 Da LogP 1.08 TPSA 27.7 ✓ Ro5 ✓ Clean CCOCCOCCOCC
PEP
5JVL
P22221 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-]

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.