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gabD gabD proA proA betA betA betB betB mhpF mhpF putA putA hemA hemA adhE adhE puuC puuC feaB feaB paaZ paaZ aldA aldA patD patD fdnG fdnG fdnI fdnI ydeP ydeP sad sad astD astD gapA gapA usg usg gtrA gtrA eutE eutE epd epd yraR yraR asd asd aldB aldB fdoI fdoI fdoG fdoG argC argC fdhF fdhF
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gabDSuccinate-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)
proAGamma-glutamylphosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family. (417 aa)
betACholine dehydrogenase, a flavoprotein; Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. Belongs to the GMC oxidoreductase family. (556 aa)
betBBetaine aldehyde dehydrogenase, NAD-dependent; Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid. It is highly specific for betaine and has a significantly higher affinity for NAD than for NADP. (490 aa)
mhpFacetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. (316 aa)
putADelta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon; In the C-terminal section; belongs to the aldehyde dehydrogenase family. (1320 aa)
hemAGlutamyl tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA. (418 aa)
adhEAcetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. (891 aa)
puuCGamma-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)
feaBPhenylacetaldehyde dehydrogenase; Acts almost equally well on phenylacetaldehyde, 4- hydroxyphenylacetaldehyde and 3,4-dihydroxyphenylacetaldehyde. (499 aa)
paaZoxepin-CoA hydrolase and 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase; Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)- ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C- terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reactive 3-oxo-5,6- dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6- dehydrosuberyl-CoA. Can also use crotonyl-CoA [...] (681 aa)
aldAAldehyde dehydrogenase A, NAD-linked; Acts on lactaldehyde as well as other aldehydes. (479 aa)
patDGamma-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)
fdnGFormate dehydrogenase-N, alpha subunit, nitrate-inducible; Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). (1015 aa)
fdnIFormate dehydrogenase-N, cytochrome B556 (gamma) subunit, nitrate-inducible; Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). (217 aa)
ydePPutative oxidoreductase; Probably involved in acid resistance. Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (759 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)
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)
gapAGlyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. (331 aa)
usgPutative semialdehyde dehydrogenase; Putative PTS system enzyme II A component. (337 aa)
gtrACPS-53 (KpLE1) prophage; Involved in O antigen modification. Involved in the translocation of bactoprenol-linked glucose across the cytoplasmic membrane (By similarity); Belongs to the GtrA family. (120 aa)
eutEAldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. (467 aa)
epdD-erythrose 4-phosphate dehydrogenase; Catalyzes the NAD-dependent conversion of D-erythrose 4- phosphate to 4-phosphoerythronate. (339 aa)
yraRPutative nucleoside-diphosphate-sugar epimerase; To yeast YER004W. (211 aa)
asdAspartate-semialdehyde dehydrogenase, NAD(P)-binding; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate. (367 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)
fdoIFormate dehydrogenase-O, cytochrome b556 subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase. (211 aa)
fdoGFormate dehydrogenase-O, large subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1016 aa)
argCN-acetyl-gamma-glutamylphosphate reductase, NAD(P)-binding; Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. (334 aa)
fdhFFormate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. (715 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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