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cadA cadA aldB aldB patA patA gabT gabT eutE eutE astD astD sad sad gadB gadB gadC gadC puuE puuE puuA puuA speF speF tesB tesB ldcC ldcC speE speE
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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cadALysine decarboxylase, acid-inducible; Inducible lysine decarboxylase that catalyzes the proton- dependent decarboxylation of L-lysine to produce the polyamine cadaverine and carbon dioxide. Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by- products of carbohydrate fermentation. Belongs to the Orn/Lys/Arg decarboxylase class-I family. (715 aa)
aldBAldehyde dehydrogenase B; Catalyzes the NADP-dependent oxidation of diverse aldehydes such as chloroacetaldehyde, acetaldehyde, propionaldehyde, benzaldehyde, mafosfamide, 4-hydroperoxycyclophosphamide. Its preferred substrates are acetaldehyde and chloroacetaldehyde. (512 aa)
patAPutrescine:2-oxoglutaric acid aminotransferase, PLP-dependent; Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4- aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source. Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cad [...] (459 aa)
gabT4-aminobutyrate aminotransferase, PLP-dependent; Pyridoxal phosphate-dependent enzyme that catalyzes transamination between primary amines and alpha-keto acids. Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA) and glutamate. Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth. Also catalyzes the conversion of 5-aminovalerate to glutarate semialdehyde, as part of a L-lysine degradation pathway that proceeds via cadaverine, [...] (426 aa)
eutEAldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. (467 aa)
astDSuccinylglutamic semialdehyde dehydrogenase; Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. Also shows activity with decanal or succinic semialdehyde as the electron donor and NAD as the electron acceptor. No activity is detected with NADP as the electron acceptor. Therefore, is an aldehyde dehydrogenase with broad substrate specificity. (492 aa)
sadSuccinate semialdehyde dehydrogenase, NAD(P)+-dependent; Catalyzes the NAD(+)-dependent oxidation of succinate semialdehyde to succinate. It acts preferentially with NAD as cosubstrate but can also use NADP. Prevents the toxic accumulation of succinate semialdehyde (SSA) and plays an important role when arginine and putrescine are used as the sole nitrogen or carbon sources. (462 aa)
gadBGlutamate decarboxylase B, PLP-dependent; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria; Belongs to the group II decarboxylase family. (466 aa)
gadCGlutamate:gamma-aminobutyric acid antiporter; Involved in glutamate-dependent acid resistance. Imports glutamate inside the cell while simultaneously exporting to the periplasm the GABA produced by GadA and GadB. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria; Belongs to the amino acid-polyamine-organocation (APC) superfamily. Glutamate:GABA [...] (511 aa)
puuE4-aminobutyrate aminotransferase, PLP-dependent; Catalyzes the transfer of the amino group from gamma- aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). PuuE is important for utilization of putrescine as the sole nitrogen or carbon source; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (421 aa)
puuAGlutamate--putrescine ligase; Involved in the breakdown of putrescine via the biosynthesis of gamma-L-glutamylputrescine. It is able to use several diamines, spermidine and spermine. Absolutely essential to utilize putrescine as both nitrogen and carbon sources and to decrease the toxicity of putrescine, which can lead to inhibition of cell growth and protein synthesis; Belongs to the glutamine synthetase family. (472 aa)
speFOrnithine decarboxylase isozyme, inducible; Protein involved in polyamine biosynthetic process; Belongs to the Orn/Lys/Arg decarboxylase class-I family. (732 aa)
tesBacyl-CoA thioesterase 2; Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known; Belongs to the C/M/P thioester hydrolase family. (286 aa)
ldcCLysine decarboxylase 2, constitutive; Plays a role in lysine utilization by acting as a lysine decarboxylase. (713 aa)
speESpermidine synthase (putrescine aminopropyltransferase); Involved in the biosynthesis of polyamines which play a significant role in the structural and functional organization in the chromoid of E.coli by compacting DNA and neutralizing negative charges. Catalyzes the irreversible transfer (ping-pong mechanism) of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. Cadaverine (1,5-diaminopentane) and spermidine can also be used as the propylamine acceptor. (288 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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