Proteins

Genome: NC_002516.2

Description: Pseudomonas aeruginosa PAO1, complete genome

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5572 / 5572 proteins

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# Protein Description Gene Structure EC GO Metabolism Druggability FPocket druggability score for the preferred structure (0–1): experimental structure when available, otherwise predicted model. ≥ 0.7 highly druggable · ≥ 0.4 moderately druggable · < 0.4 low druggability. Human off-target BLASTP against the human proteome. Hit means at least one human match was detected at e-value <= 1e-5. Prefer No hit for pathogen-selective targets. Human identity (%) Best human BLAST identity percentage. Human E-value Best human BLAST E-value.
2776 PA1094 B-type flagellar hook-associated protein fliD, PA1094 Experimental + AlphaFold –
GO:0009421The proteinaceous structure at the distal tip of the bacterial-type flagellar filament. GO:0009424The portion of the bacterial-type flagellum that connects the filament to the basal body. GO:0005576The 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. +36 total
No map 0.736 No Hit N/A —
2777 PA1028 oxidoreductase PA1028 AlphaFold –
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0016491Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
No map 0.736 No Hit N/A —
2778 PA0871 pterin-4-alpha-carbinolamine dehydratase phhB, PA0871 AlphaFold
4.2.1.96
GO:0008124Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O. GO:0006729The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.
No map 0.736 Hit 33.7% 8.51e-07
2779 PA0853 oxidoreductase PA0853 AlphaFold –
GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0003955Catalysis of the reaction: NAD(P)H + H+ + a quinone = NAD(P)+ + a quinol.
No map 0.736 Hit 39.7% 1.40e-09
2780 PA0480 3-oxoadipate enol-lactonase PA0480 Experimental + AlphaFold –
GO:0047570Catalysis of the reaction: 3-oxoadipate enol-lactone + H2O = 3-oxoadipate. GO:0042952A pathway of aromatic compound degradation by ortho-cleavage; one branch converts protocatechuate, derived from phenolic compounds, to beta-ketoadipate, and the other branch converts catechol, generated from various aromatic hydrocarbons, amino aromatics, and lignin monomers, also to beta-ketoadipate. Two additional steps accomplish the conversion of beta-ketoadipate to tricarboxylic acid cycle intermediates.
No map 0.736 Hit 34.1% 2.42e-07
2781 PA0350 dihydrofolate reductase folA, PA0350 AlphaFold
1.5.1.3
GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004146Catalysis of the reaction: 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+. GO:0050661Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. +69 total
No map 0.736 Hit 40.7% 4.70e-09
2782 PA5454 oxidoreductase Rmd rmd, PA5454 Experimental + AlphaFold
1.1.1.281
GO:0033705Catalysis of the reaction: GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+. GO:0070402Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. GO:0016491Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. +36 total
No map 0.735 Hit 36.7% 9.25e-08
2783 PA5312 aldehyde dehydrogenase PA5312 Experimental + AlphaFold –
GO:0004030Catalysis of the reaction: an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+. GO:0016620Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP. GO:0016491Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
No map 0.735 Hit 50.0% 6.21e-07
2784 PA4776 two-component regulator system response regulator PmrA pmrA, PA4776 AlphaFold –
GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0032993A macromolecular complex containing both protein and DNA molecules. GO:0000156Responds to a phosphorelay sensor to initiate a change in cell state or activity. The activity of the response regulator is regulated by transfer of a phosphate from a histidine residue in the sensor, to an aspartate residue in the response regulator. Many but not all response regulators act as transcriptional regulators to elicit a response. +47 total
No map 0.735 No Hit N/A —
2785 PA4145a hypothetical protein ColabFold –
GO:0016020A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0006865The directed movement of amino acids, organic acids containing one or more amino substituents, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
No map 0.735 No Hit N/A —
2786 PA3934 hypothetical protein PA3934 Experimental + AlphaFold –
GO:0016020A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0035673Enables the transfer of oligopeptides from one side of a membrane to the other. Oligopeptides are molecules that contain a small number (2 to 20) of amino-acid residues connected by peptide linkages.
No map 0.735 No Hit N/A —
2787 PA3663 hypothetical protein PA3663 AlphaFold – – No map 0.735 No Hit N/A —
2788 PA2832 thiopurine S-methyltransferase PA2832, tpm AlphaFold
2.1.1.67
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0008119Catalysis of the reaction: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. GO:0032259The process in which a methyl group is covalently attached to a molecule. +25 total
No map 0.735 Hit 30.9% 4.02e-29
2789 PA2765 hypothetical protein PA2765 AlphaFold –
GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0020037Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. GO:0046872Binding to a metal ion. +14 total
No map 0.735 No Hit N/A —
2790 PA2630 hypothetical protein PA2630 AlphaFold –
GO:0016706Catalysis of the reaction: A + 2-oxoglutarate + O2 = B + succinate + CO2. This is an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from 2-oxoglutarate and one other donor, and one atom of oxygen is incorporated into each donor. GO:0046872Binding to a metal ion.
No map 0.735 No Hit N/A —
2791 PA2294 ABC transporter ATP-binding protein PA2294 AlphaFold –
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016887Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
No map 0.735 Hit 34.4% 7.84e-16
2792 PA1829 hypothetical protein PA1829 AlphaFold – – No map 0.735 Hit 38.3% 6.00e-17
2793 PA1789 hypothetical protein PA1789 Experimental + AlphaFold –
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
No map 0.735 No Hit N/A —
2794 PA1604 hypothetical protein PA1604 AlphaFold – – No map 0.735 No Hit N/A —
2795 PA0420 adenosylmethionine--8-amino-7-oxononanoate aminotransferase BioA bioA, PA0420 AlphaFold
2.6.1.62
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0004015Catalysis of the reaction: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate. GO:0030170Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. +36 total
No map 0.735 Hit 28.8% 1.22e-38
2796 PA4897 hypothetical protein PA4897 AlphaFold –
GO:0009279A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures. GO:0019867The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites. GO:0033214A process in which iron (Fe3+) is solubilized by ferric iron-specific chelators, known as siderophores is imported into the cell by transmembrane transport or endocytosis.
No map 0.734 No Hit N/A —
2797 PA4450 UDP-N-acetylglucosamine 1-carboxyvinyltransferase murA, PA4450 Experimental + AlphaFold
2.5.1.7
GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0008760Catalysis of the reaction: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine. GO:0051301The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. +69 total
No map 0.734 No Hit N/A —
2798 PA4399 hypothetical protein PA4399 AlphaFold
2.5.1.17
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0008817Catalysis of the reaction: 2 ATP + 2 corrinoid + reduced [electron-transfer flavoprotein] = 2 adenosylcorrinoid + 3 H+ + oxidized [electron-transfer flavoprotein] + 2 triphosphate. The corrinoid can be cob(II)yrinate a,c diamide, cob(II)inamide or cob(II)alamin. GO:0009236The chemical reactions and pathways resulting in the formation of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
No map 0.734 Hit 47.7% 2.93e-06
2799 PA3648 outer membrane protein Opr86 PA3648, opr86, bamA AlphaFold –
GO:1990063Protein complex which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. In E. coli it is composed of BamABCDE, of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. BamA interacts directly with BamB and the BamCDE subcomplex. GO:0009279A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures. GO:0043165The assembly of an outer membrane of the type formed in Gram-negative bacteria. This membrane is enriched in polysaccharide and protein, and the outer leaflet of the membrane contains specific lipopolysaccharide structures. +36 total
No map 0.734 No Hit N/A —
2800 PA2848 transcriptional regulator PA2848 AlphaFold –
GO:0003700A transcription regulator activity that modulates transcription of gene sets via selective and non-covalent binding to a specific double-stranded genomic DNA sequence (sometimes referred to as a motif) within a cis-regulatory region. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units, and include bacterial operons. GO:0000976Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon. GO:0006355Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
No map 0.734 No Hit N/A —
Page of 223 · 5572 total proteins