Protein profile

PA3635

enolase

Genome: NC_002516.2

Gene: PA3635 eno Structure source: AlphaFold UniProt Q9HXZ5
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Amino acids 429
Annotations 7
Features 43
PDB binders 5

Overview

Basic information about this protein and its source genome.

Accession
PA3635
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3635 eno
Status
annotated
Amino acids
429
Structure source
AlphaFold
EC
4.2.1.11
GO
GO:0009986 The external part of the cell wall and/or plasma membrane. GO:0005576 The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. GO:0000015 A multimeric enzyme complex, usually a dimer or an octamer, that catalyzes the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate and water. GO:0000287 Binding to a magnesium (Mg) ion. GO:0004634 Catalysis of the reaction: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O. GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
64.138
Human E-value
4.66e-48
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

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:0009986 The external part of the cell wall and/or plasma membrane.
  • GO:0005576 The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
  • GO:0000015 A multimeric enzyme complex, usually a dimer or an octamer, that catalyzes the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate and water.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:0004634 Catalysis of the reaction: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
  • GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records
Show feature table
Start End DB Term Name
3 138 SUPERFAMILY SSF54826 Enolase N-terminal domain-like
3 138 InterPro IPR029017 Enolase-like, N-terminal
367 384 PRINTS PR00148 Enolase signature
367 384 InterPro IPR000941 Enolase
107 123 PRINTS PR00148 Enolase signature
107 123 InterPro IPR000941 Enolase
37 51 PRINTS PR00148 Enolase signature
37 51 InterPro IPR000941 Enolase
165 178 PRINTS PR00148 Enolase signature
165 178 InterPro IPR000941 Enolase
338 352 PRINTS PR00148 Enolase signature
338 352 InterPro IPR000941 Enolase
315 326 PRINTS PR00148 Enolase signature
315 326 InterPro IPR000941 Enolase
128 429 FunFam G3DSA:3.20.20.120:FF:000001 Enolase
128 429 Gene3D G3DSA:3.20.20.120 -
128 429 InterPro IPR036849 Enolase-like, C-terminal domain superfamily
4 134 Pfam PF03952 Enolase, N-terminal domain
4 134 InterPro IPR020811 Enolase, N-terminal
6 414 CDD cd03313 enolase
6 414 InterPro IPR000941 Enolase
3 424 PANTHER PTHR11902 ENOLASE
3 424 InterPro IPR000941 Enolase
4 427 NCBIfam TIGR01060 phosphopyruvate hydratase
4 427 InterPro IPR000941 Enolase
1 127 Gene3D G3DSA:3.30.390.10 -
1 127 InterPro IPR029017 Enolase-like, N-terminal
4 134 SMART SM01193 Enolase_N_3
144 426 Pfam PF00113 Enolase, C-terminal TIM barrel domain
144 426 InterPro IPR020810 Enolase, C-terminal TIM barrel domain
2 415 SFLD SFLDF00002 enolase
2 415 InterPro IPR000941 Enolase
1 429 PIRSF PIRSF001400 Enolase
1 429 InterPro IPR000941 Enolase
2 415 SFLD SFLDG00178 enolase
2 415 Hamap MF_00318 Enolase [eno].
338 351 ProSitePatterns PS00164 Enolase signature.
338 351 InterPro IPR020809 Enolase, conserved site
143 429 SMART SM01192 Enolase_C_3
143 429 InterPro IPR020810 Enolase, C-terminal TIM barrel domain
143 427 SUPERFAMILY SSF51604 Enolase C-terminal domain-like
143 427 InterPro IPR036849 Enolase-like, C-terminal domain superfamily
1 127 FunFam G3DSA:3.30.390.10:FF:000001 Enolase

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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No pockets are loaded yet for the displayed AlphaFold model PA3635 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.

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Structural evidence

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA3635
AlphaFold — — full sequence — Viewing

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.

39 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
2PG
6BFY
P0A6P9 186.1 Da LogP -1.46 TPSA 124.3 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)OP(=O)(O)O)O
4NG
6D3Q
P0A6P9 197.1 Da LogP -1.53 TPSA 118.3 ✓ Ro5 ✓ Clean C1[C@@H](C(=O)N([C@H]1O)O)P(=O)(O)O
KVM
6NPF
P0A6P9 195.1 Da LogP -1.32 TPSA 115.1 ✓ Ro5 ✓ Clean C1[C@@H](C(=O)N(C1=O)O)P(=O)(O)O
PEP
4Z17
A9WCM4 168.0 Da LogP -0.31 TPSA 104.1 ✓ Ro5 ✓ Clean C=C(C(=O)O)OP(=O)(O)O
TLA
6NPF
P0A6P9 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=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.