Proteins

Genome: KpKP13

Description: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence

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5192 / 5842 proteins Structure: AlphaFold

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Structure: AlphaFold ×
# 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.
2726 KP13_25192 3-oxoadipate enol-lactonase 2 AlphaFold + ColabFold –
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 0.536 Hit 29.4% 8.02e-07
2727 KP13_04886 4-hydroxythreonine-4-phosphate dehydrogenase pdxA AlphaFold + ColabFold –
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.
No map 0.536 No Hit 0.0% —
2728 KP13_04586 Coenzyme PQQ synthesis protein E pqqE AlphaFold + ColabFold
1.21.98.4
GO:0051539Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0046872Binding to a metal ion. 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. +710 total
No map 0.536 No Hit 0.0% —
2729 KP13_04237 NAD(P)-binding domain-containing protein AlphaFold + ColabFold – – No map 0.536 Hit 25.0% 2.45e-13
2730 KP13_00454 Protein phnI phnI AlphaFold + ColabFold –
GO:0019634The chemical reactions and pathways involving phosphonates, any organic compounds containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Metabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.
No map 0.536 No Hit 0.0% —
2731 KP13_31972 hypothetical protein AlphaFold + ColabFold – – No map 0.535 No Hit 0.0% —
2732 KP13_04578 AFG1-family ATPase protein AlphaFold + ColabFold
1.11.1.6
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:0032153The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles. +36 total
No map 0.535 Hit 46.8% 9.61e-12
2733 KP13_03192 Periplasmic beta-glucosidase bglX AlphaFold + ColabFold
3.2.1.21
GO:0005975The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. GO:0004553Catalysis of the hydrolysis of any O-glycosyl bond. GO:0042597The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). +25 total
No map 0.535 No Hit 0.0% —
2734 KP13_02298 Threonine-phosphate decarboxylase cobD AlphaFold + ColabFold
4.1.1.81
GO:0030170Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0009058A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones. 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. +25 total
No map 0.535 No Hit 0.0% —
2735 KP13_00389 Replicative DNA helicase dnaB AlphaFold + ColabFold
5.6.2.3
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:0006260The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. GO:0003678Unwinding of a DNA helix, driven by ATP hydrolysis. +710 total
No map 0.535 No Hit 0.0% —
2736 KP13_31541 DNA mismatch repair protein mutS mutS AlphaFold + ColabFold –
GO:0140664A molecule that recognises toxic DNA structures, and initiates a signaling response, driven by ATP hydrolysis. GO:0006298A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination. GO:0030983Binding to a double-stranded DNA region containing one or more mismatches. +36 total
No map 0.534 Hit 61.5% 6.97e-10
2737 KP13_04967 Phenylacetic acid degradation protein paaA paaA AlphaFold + ColabFold –
GO:0097266Catalysis of the reaction: phenylacetyl-CoA + H+ + NADPH + O2 = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP+. GO:0010124The chemical reactions and pathways resulting in the breakdown of phenylacetate. GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
No map 0.534 No Hit 0.0% —
2738 KP13_05181 Glyceraldehyde-3-phosphate dehydrogenase gap AlphaFold + ColabFold –
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: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: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. +25 total
No map 0.533 Hit 50.0% 1.34e-107
2739 KP13_04135 Tellurite resistance TerY-type protein AlphaFold + ColabFold – – No map 0.533 No Hit 0.0% —
2740 KP13_01239 hypothetical protein AlphaFold + ColabFold – – No map 0.533 No Hit 0.0% —
2741 KP13_01024 Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta accD AlphaFold + ColabFold
2.1.3.15
GO:0003989Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. GO:0009317A protein complex that catalyzes the first step in long-chain fatty acid biosynthesis. For example, in E. coli the complex is heterohexameric and composed of biotin carbonyl carrier protein, biotin carboxylase and the acetate CoA-transferase complex. 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. +58 total
No map 0.533 Hit 29.1% 8.61e-06
2742 KP13_05719 Propanediol utilization protein pduA AlphaFold + ColabFold –
GO:0031469An organelle found in bacteria consisting of a proteinaceous coat containing metabolic enzymes whose purpose is the sequestration or concentration of metabolites and which has the appearance of a polygonal granule by electron microscopy.
No map 0.532 No Hit 0.0% —
2743 KP13_05272 putative isomerase AlphaFold + ColabFold –
GO:0009058A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones. 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:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. +14 total
No map 0.532 Hit 36.4% 1.06e-42
2744 KP13_04721 Nitrate transport protein nrtA nrtA AlphaFold + ColabFold –
GO:0012505A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
No map 0.532 No Hit 0.0% —
2745 KP13_03907 putative HTH-type transcriptional regulator AlphaFold + ColabFold –
GO:0003677Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
No map 0.532 No Hit 0.0% —
2746 KP13_01814 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase dapD AlphaFold + ColabFold
2.3.1.117
GO:0009089OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate. GO:0016740Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. GO:0008666Catalysis of the reaction: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = L-2-succinylamino-6-oxopimelate + CoA. +36 total
No map 0.532 No Hit 0.0% —
2747 KP13_15895 Agmatinase AlphaFold + ColabFold
3.5.3.11
GO:0016813Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amidine, a compound of the form R-C(=NH)-NH2. GO:0046872Binding to a metal ion. GO:0008783Catalysis of the reaction: agmatine + H2O = putrescine + urea. +25 total
No map 0.531 Hit 61.4% 5.34e-136
2748 KP13_05528 hypothetical protein AlphaFold + ColabFold – – No map 0.531 No Hit 0.0% —
2749 KP13_05352 tRNA threonylcarbamoyladenosine biosynthesis protein AlphaFold + ColabFold –
GO:0003725Binding to double-stranded RNA.
No map 0.531 Hit 26.8% 8.15e-06
2750 KP13_04624 hypothetical protein AlphaFold + ColabFold – – No map 0.531 No Hit 0.0% —
Page of 208 · 5192 total proteins