Proteins

Genome: KpATCC43816

Description: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome

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5081 proteins

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# Protein Description Gene Structure EC GO 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.
1 VK055_2464 guanosine monophosphate reductase guaC AlphaFold + ColabFold –
GO:0003920Catalysis of the reaction: IMP + NADP+ + NH4 = GMP + 2 H+ + NADPH. GO:0003824Catalysis 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: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. +25 total
0.659 Hit 87.5% 2.28e-18
2 VK055_3750 translation elongation factor Tu tuf2 AlphaFold + ColabFold
3.6.5.3
GO:0003746Functions in chain elongation during polypeptide synthesis at the ribosome. GO:0005525Binding to GTP, guanosine triphosphate. GO:0006414The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis. +58 total
0.781 Hit 81.2% 1.64e-09
3 VK055_3117 translation elongation factor Tu tuf AlphaFold + ColabFold –
GO:0003746Functions in chain elongation during polypeptide synthesis at the ribosome. GO:0005525Binding to GTP, guanosine triphosphate. GO:0006414The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis. +14 total
0.781 Hit 81.2% 1.64e-09
4 VK055_3327 tRNA uridine 5-carboxymethylaminomethyl modification enzyme GidA gidA AlphaFold + ColabFold –
GO:0008033The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group. GO:0050660Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0002098The process in which a uridine at position 34 of a tRNA is post-transcriptionally modified. The wobble nucleoside of the tRNA sequence (position 34) corresponds to the first position of the anticodon. +36 total
0.616 Hit 76.3% 1.92e-06
5 VK055_4640 scaffold protein involved in iron-sulfur cluster assembly AlphaFold + ColabFold –
GO:0016226The incorporation of iron and exogenous sulfur into a metallo-sulfur cluster. GO:0005506Binding to an iron (Fe) ion. GO:0051536Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
0.181 Hit 75.4% 2.18e-69
6 VK055_2930 chaperonin GroL groL AlphaFold + ColabFold
5.6.1.7
GO:0006457The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0140662Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. +47 total
0.209 Hit 75.0% 5.59e-08
7 VK055_1858 leucine--tRNA ligase leuS AlphaFold + ColabFold
6.1.1.4
GO:0002161The hydrolysis of an incorrectly aminoacylated tRNA. GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0004812Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP. +58 total
0.782 Hit 73.0% 9.14e-12
8 VK055_3336 ATP synthase F1, beta subunit atpD AlphaFold + ColabFold
7.1.2.2
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0015986The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a membrane to generate an electrochemical gradient (proton-motive force). GO:0045261OBSOLETE. The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled. +69 total
0.523 Hit 71.0% 0.00e+00
9 VK055_2849 methionine sulfoxide reductase A msrA AlphaFold + ColabFold
1.8.4.11
GO:0008113Catalysis of the reaction: L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L-methionyl-(S)-S-oxide-[protein] + [thioredoxin]-dithiol. GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0033744Catalysis of the reaction: [thioredoxin]-disulfide + L-methionine + H2O = L-methionine (S)-S-oxide + [thioredoxin]-dithiol. +14 total
0.021 Hit 70.7% 3.01e-41
10 VK055_4639 cysteine desulfurase IscS iscS AlphaFold + ColabFold
2.8.1.7
GO:0031071Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine. GO:0003824Catalysis 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:0044571The incorporation of two iron atoms and two sulfur atoms into an iron-sulfur cluster. +47 total
0.469 Hit 70.7% 1.30e-29
11 VK055_3061 phosphoglucose isomerase family protein AlphaFold + ColabFold
5.3.1.9
GO:0004347Catalysis of the reaction: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate. GO:0006094The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol. GO:0097367Binding to a carbohydrate derivative. +58 total
0.764 Hit 70.2% 0.00e+00
12 VK055_3095 uroporphyrinogen decarboxylase hemE AlphaFold + ColabFold
4.1.1.37
GO:0004853Catalysis of the reaction: uroporphyrinogen-III = coproporphyrinogen + 4 CO2. GO:0006779The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group. GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. +14 total
0.095 Hit 70.2% 4.41e-21
13 VK055_3227 argininosuccinate lyase argH AlphaFold + ColabFold
4.3.2.1
GO:0042450OBSOLETE. The chemical reactions and pathways resulting in the formation of arginine (2-amino-5-guanidinopentanoic acid) via the intermediate compound ornithine. GO:0003824Catalysis 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:0004056Catalysis of the reaction: N-(L-arginino)succinate = fumarate + L-arginine. +14 total
0.592 Hit 70.0% 9.84e-18
14 VK055_1830 glutamine--tRNA ligase glnS AlphaFold + ColabFold
6.1.1.18
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0043039The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules. GO:0004819Catalysis of the reaction: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). +811 total
0.933 Hit 69.7% 2.15e-07
15 VK055_1263 glyceraldehyde-3-phosphate dehydrogenase, type I gap2 AlphaFold + ColabFold
1.2.1.-
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. GO:0051287Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. 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. +36 total
0.502 Hit 69.7% 7.91e-128
16 VK055_1797 succinate dehydrogenase iron-sulfur protein sdhB AlphaFold + ColabFold
1.3.5.1
GO:0051536Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0006099A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. 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. +710 total
0.437 Hit 68.9% 1.16e-42
17 VK055_1793 succinyl-CoA synthetase, alpha subunit sucD AlphaFold + ColabFold
6.2.1.5
GO:0003824Catalysis 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:0009361A heterodimeric enzyme complex, composed of an alpha and beta chain, most usually found in (but not limited to) bacteria. Functions in the TCA cycle, hydrolyzing succinyl-CoA into succinate and CoA, thereby forming ATP. GO:0000166Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. +36 total
0.867 Hit 68.7% 5.63e-64
18 VK055_2353 D-methionine ABC transporter, ATP-binding protein metN AlphaFold + ColabFold –
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0048473The process in which D-methionine is transported across a lipid bilayer, from one side of a membrane to the other. GO:0033232Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + D-methionine(out/in) = ADP + phosphate + D-methionine(in/out). +36 total
0.434 Hit 67.6% 1.01e-07
19 VK055_4144 glycine dehydrogenase gcvP AlphaFold + ColabFold
1.4.4.2
GO:0006546The chemical reactions and pathways resulting in the breakdown of glycine. GO:0003824Catalysis 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:0006544The chemical reactions and pathways involving glycine, aminoethanoic acid. +69 total
0.961 Hit 67.3% 2.72e-20
20 VK055_0526 S-(hydroxymethyl)glutathione dehydrogenase/classIII alcohol dehydrogenase AlphaFold + ColabFold
1.1.1.284
GO:0008270Binding to a zinc ion (Zn). GO:0051903Catalysis of the reaction: S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+. 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. +710 total
0.288 Hit 67.3% 4.95e-46
21 VK055_4093 alanine racemase, N-terminal domain protein AlphaFold + ColabFold –
GO:0030170Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
0.873 Hit 66.7% 9.32e-06
22 VK055_2560 chaperone protein DnaK dnaK AlphaFold + ColabFold –
GO:0006457The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0140662Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. +25 total
0.425 Hit 65.9% 4.46e-54
23 VK055_2094 htpG htpG AlphaFold + ColabFold –
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0006457The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. GO:0140662Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. +36 total
0.501 Hit 65.8% 2.16e-10
24 VK055_1374 3-oxoacyl-[acyl-carrier-protein] reductase fabG Experimental + ColabFold
1.1.1.100
GO:0006633The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. GO:0051287Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. 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. +25 total
0.42 Hit 65.6% 2.44e-06
25 VK055_0835 ABC transporter family protein AlphaFold + ColabFold –
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. GO:0005886The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. +14 total
0.497 Hit 64.9% 1.57e-07
Page of 204 · 5081 total proteins