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speD | S-adenosylmethionine decarboxylase; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. (264 aa) | ||||
speE | Spermidine 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) | ||||
ldcC | Lysine decarboxylase 2, constitutive; Plays a role in lysine utilization by acting as a lysine decarboxylase. (713 aa) | ||||
potE | Putrescine transporter PotE; Catalyzes both the uptake and excretion of putrescine. The uptake of putrescine is dependent on the membrane potential and the excretion involves putrescine-ornithine antiporter activity. (439 aa) | ||||
speF | Ornithine decarboxylase isozyme, inducible; Protein involved in polyamine biosynthetic process; Belongs to the Orn/Lys/Arg decarboxylase class-I family. (732 aa) | ||||
puuP | Putrescine importer; Involved in the uptake of putrescine. Belongs to the amino acid-polyamine-organocation (APC) superfamily. (461 aa) | ||||
puuA | Glutamate--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) | ||||
puuD | Gamma-glutamyl-gamma-aminobutyrate hydrolase; Involved in the breakdown of putrescine via hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate. (254 aa) | ||||
puuR | Repressor for the divergent puu operons, putrescine inducible; Represses puuA, puuD and puuP. (185 aa) | ||||
puuC | Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Catalyzes the oxidation of 3-hydroxypropionaldehyde (3-HPA) to 3-hydroxypropionic acid (3-HP). It acts preferentially with NAD but can also use NADP. 3-HPA appears to be the most suitable substrate for PuuC followed by isovaleraldehyde, propionaldehyde, butyraldehyde, and valeraldehyde. It might play a role in propionate and/or acetic acid metabolisms. Also involved in the breakdown of putrescine through the oxidation of gamma-Glu-gamma-aminobutyraldehyde to gamma-Glu-gamma-aminobutyrate (gamma-Glu-GABA). (495 aa) | ||||
puuB | Gamma-glutamylputrescine oxidoreductase; Involved in the breakdown of putrescine via the oxidation of L-glutamylputrescine. (426 aa) | ||||
puuE | 4-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) | ||||
patD | Gamma-aminobutyraldehyde dehydrogenase; Catalyzes the oxidation 4-aminobutanal (gamma- aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. Can also oxidize n-alkyl medium-chain aldehydes, bu [...] (474 aa) | ||||
ddpX | D-ala-D-ala dipeptidase, Zn-dependent; Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. May have a role in cell-wall turnover. (193 aa) | ||||
sad | Succinate 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) | ||||
astE | Succinylglutamate desuccinylase; Transforms N(2)-succinylglutamate into succinate and glutamate; Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily. (322 aa) | ||||
astB | Succinylarginine dihydrolase; Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)- succinylornithine, ammonia and CO(2). (447 aa) | ||||
astD | Succinylglutamic 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) | ||||
astA | Arginine succinyltransferase; Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. (344 aa) | ||||
astC | Succinylornithine transaminase, PLP-dependent; Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily. (406 aa) | ||||
lysP | Lysine transporter; Permease that is involved in the transport across the cytoplasmic membrane of lysine; Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family. (489 aa) | ||||
csiD | tRNA-Ile; Acts as an alpha-ketoglutarate-dependent dioxygenase catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate (L2HG) in the stationary phase of E.coli. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2- hydroxyglutarate. Other dicarboxylic acids (oxalate, malonate, succinate, adipate, and pimelate) are not substrates for this enzyme. (325 aa) | ||||
lhgO | L-2-hydroxyglutarate oxidase; Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG) to alpha-ketoglutarate and couples to the respiratory chain by feeding electrons from the reaction into the membrane quinone pool. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (422 aa) | ||||
gabD | Succinate-semialdehyde dehydrogenase I, NADP-dependent; Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. 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 glutarate semialdehyde to glutarate, as part of a L- lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (482 aa) | ||||
gabT | 4-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) | ||||
gabP | Gamma-aminobutyrate transporter; Transporter for GABA; Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family. (466 aa) | ||||
csiR | Transcriptional repressor of csiD; Negatively regulates the expression of the glaH-lhgD-gabDTP operon in a temporal manner during entry into stationary phase or during the first few hours of carbon starvation. Thereby is involved in the regulation of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2- hydroxyglutarate. Binds to two primary and two secondary sites in the promoter region of the glaH operon with the consensus sequences TTGTN5TTTT and ATGTN5TTTT of the primary sites, each separated by six nucleotides. (220 aa) | ||||
speB | Agmatinase; Catalyzes the formation of putrescine from agmatine. (306 aa) | ||||
speA | Biosynthetic arginine decarboxylase, PLP-binding; Catalyzes the biosynthesis of agmatine from arginine. Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. (658 aa) | ||||
speC | Ornithine decarboxylase, constitutive; Ornithine decarboxylase isozyme; Protein involved in polyamine biosynthetic process. (711 aa) | ||||
patA | Putrescine: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) | ||||
viaA | Stimulator of RavA ATPase activity; von Willebrand factor domain protein. (483 aa) | ||||
ravA | Hexameric AAA+ MoxR family ATPase, putative molecular chaperone; Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone. (498 aa) | ||||
adiA | Arginine decarboxylase; ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins; Belongs to the Orn/Lys/Arg decarboxylase class-I family. (755 aa) | ||||
cadA | Lysine 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) | ||||
cadB | Putative lysine/cadaverine transporter; Probable cadaverine/lysine antiporter or part of it. (444 aa) | ||||
cadC | cadBA operon transcriptional activator; Required for Pcad induction, a promoter upstream of cadBA that is responsible for the pH-regulated expression of CadA and CadB. Probably acts as an activating transcription factor. (512 aa) |