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nadC nadC ushA ushA nadD nadD nadA nadA pncB pncB cobB cobB sad sad pntB pntB pntA pntA nadE nadE pncA pncA nadB nadB nadK nadK gabD gabD pncC pncC umpG umpG mazG mazG yrfG yrfG sthA sthA nudC nudC yjjG yjjG deoD deoD nadR nadR
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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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nadCQuinolinate phosphoribosyltransferase; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (297 aa)
ushABifunctional UDP-sugar hydrolase/5'-nucleotidase; Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell. (550 aa)
nadDNicotinic acid mononucleotide adenylyltransferase, NAD(P)-dependent; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). Belongs to the NadD family. (213 aa)
nadAQuinolinate synthase, subunit A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. Belongs to the quinolinate synthase A family. Type 1 subfamily. (347 aa)
pncBNicotinate phosphoribosyltransferase; Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP; Belongs to the NAPRTase family. (400 aa)
cobBDeacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily. (242 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)
pntBPyridine nucleotide transhydrogenase, beta subunit; The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane; Belongs to the PNT beta subunit family. (462 aa)
pntAPyridine nucleotide transhydrogenase, alpha subunit; The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane; Belongs to the AlaDH/PNT family. (510 aa)
nadENAD synthetase, NH3/glutamine-dependent; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (275 aa)
pncANicotinamidase/pyrazinamidase; Catalyzes the deamidation of nicotinamide (NAM) into nicotinate. Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide. (213 aa)
nadBQuinolinate synthase, L-aspartate oxidase (B protein) subunit; Catalyzes the oxidation of L-aspartate to iminoaspartate. (540 aa)
nadKNAD kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (UTP, CTP, GTP, dATP, TTP) as phosphoryl donors, while nucleoside mono- or diphosphates and poly(P) can not. (292 aa)
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)
pncCNicotinamide-nucleotide amidohydrolase; Has nicotinamidemononucleotide (NMN) aminohydrolase activity, not active on other substrates; Belongs to the CinA family. PncC subfamily. (165 aa)
umpGBroad specificity 5'(3')-nucleotidase and polyphosphatase; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. Also plays [...] (253 aa)
mazGNucleoside triphosphate pyrophosphohydrolase; Involved in the regulation of bacterial cell survival under conditions of nutritional stress. Regulates the type II MazE-MazF toxin-antitoxin (TA) system which mediates programmed cell death (PCD). This is achieved by lowering the cellular concentration of (p)ppGpp produced by RelA under amino acid starvation, thus protecting the cell from the toxicity of MazF. Reduction of (p)ppGpp can be achieved by direct degradation of (p)ppGpp or by degradation of NTPs, which are substrates for (p)ppGpp synthesis by RelA. Belongs to the nucleoside trip [...] (263 aa)
yrfGGMP/IMP nucleotidase; Catalyzes the dephosphorylation of different purine nucleotides (GMP and IMP). Also hydrolyzes flavin mononucleotide (FMN). Belongs to the HAD-like hydrolase superfamily. (222 aa)
sthAPyridine nucleotide transhydrogenase, soluble; Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. (466 aa)
nudCNADH pyrophosphatase; Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates, but uniquely prefers the reduced form of NADH. (257 aa)
yjjGdUMP phosphatase; Nucleotidase that shows high phosphatase activity toward non- canonical pyrimidine nucleotides and three canonical nucleoside 5'- monophosphates (UMP, dUMP, and dTMP), and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6-phosphogluconate. Appears to function as a house-cleaning nucleotidase in vivo, since the general nucleotidase activity of YjjG allows it to protect cells against non- canonical pyrimidine derivatives such as 5-fluoro-2'-deoxyuridine, 5- fluorouridine, 5-fluoroorotate, 5-fluorouracil, and 5-aza-2'- deoxycytidine, and prevents the i [...] (225 aa)
deoDPurine nucleoside phosphorylase 1; Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. (239 aa)
nadRTrifunctional NAD biosynthesis/regulator protein NadR; This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity [...] (410 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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