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carA carA carB carB pyrH pyrH codA codA yaiE yaiE ushA ushA cmk cmk pyrD pyrD rutF rutF rutE rutE rutD rutD rutC rutC rutB rutB rutA rutA pyrC pyrC tmk tmk tdk tdk ydfG ydfG pyrF pyrF dcd dcd udk udk cdd cdd preT preT yeiA yeiA yeiK yeiK yeiN yeiN yeiC yeiC nrdA nrdA nrdB nrdB yfbR yfbR upp upp ndk ndk nrdE nrdE nrdF nrdF surE surE pyrG pyrG mazG mazG ygdH ygdH thyA thyA hyuA hyuA yrfG yrfG dut dut pyrE pyrE udp udp cpdB cpdB nrdD nrdD pyrI pyrI pyrB pyrB yjjG yjjG deoA deoA deoD deoD
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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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a 3D structure is known or predicted
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carACarbamoyl-phosphate synthetase, glutamine (small) subunit; Residues 1 to 382 of 382 are 100.00 pct identical to residues 1 to 382 of 382 from Escherichia coli K-12 Strain MG1655: B0032; Belongs to the CarA family. (382 aa)
carBCarbamoyl-phosphate synthase large subunit; Residues 1 to 1073 of 1073 are 99.72 pct identical to residues 1 to 1073 of 1073 from Escherichia coli K-12 Strain MG1655: B0033. (1073 aa)
pyrHUridylate kinase; Catalyzes the reversible phosphorylation of UMP to UDP. (241 aa)
codACytosine deaminase; Residues 1 to 427 of 427 are 99.06 pct identical to residues 1 to 427 of 427 from Escherichia coli K-12 Strain MG1655: B0337. (427 aa)
yaiEOrf, hypothetical protein; Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions. (94 aa)
ushAUDP-sugar hydrolase (5'-nucleotidase); Residues 1 to 550 of 550 are 99.27 pct identical to residues 1 to 550 of 550 from Escherichia coli K-12 Strain MG1655: B0480; Belongs to the 5'-nucleotidase family. (550 aa)
cmkCytidylate kinase; Residues 1 to 227 of 227 are 100.00 pct identical to residues 1 to 227 of 227 from Escherichia coli K-12 Strain MG1655: B0910. (227 aa)
pyrDDihydro-orotate dehydrogenase; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. (336 aa)
rutFPutative 4-hydroxyphenylacetate 3-monooxygenase; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. (152 aa)
rutEPutative enzyme; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted; Belongs to the nitroreductase family. HadB/RutE subfamily. (196 aa)
rutDPutative acetyltransferase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation (By similarity). (266 aa)
rutCOrf, hypothetical protein; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. (128 aa)
rutBPutative synthetase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2 (By similarity). (244 aa)
rutAOrf, hypothetical protein; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate (By similarity). Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. (382 aa)
pyrCDihydro-orotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. (348 aa)
tmkThymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis; Belongs to the thymidylate kinase family. (213 aa)
tdkThymidine kinase; Phosphorylates both thymidine and deoxyuridine. (205 aa)
ydfGPutative oxidoreductase; NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation sin [...] (248 aa)
pyrFOrotidine-5'-phosphate decarboxylase; Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP); Belongs to the OMP decarboxylase family. Type 1 subfamily. (245 aa)
dcd2'-deoxycytidine 5'-triphosphate deaminase; Catalyzes the deamination of dCTP to dUTP. (193 aa)
udkUridine/cytidine kinase; Residues 1 to 231 of 231 are 100.00 pct identical to residues 1 to 231 of 231 from Escherichia coli K-12 Strain MG1655: B2066; Belongs to the uridine kinase family. (231 aa)
cddCytidine/deoxycytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. (294 aa)
preTPutative oxidoreductase; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT) (By similarity). (412 aa)
yeiAPutative oxidoreductase; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT) (By similarity). (413 aa)
yeiKOrf, hypothetical protein; Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. Has a clear preference for cytidine over uridine. Strictly specific for ribonucleosides; Belongs to the IUNH family. RihB subfamily. (313 aa)
yeiNOrf, hypothetical protein; Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway; Belongs to the pseudouridine-5'-phosphate glycosidase family. (312 aa)
yeiCPutative kinase; Residues 1 to 313 of 313 are 99.04 pct identical to residues 1 to 313 of 313 from Escherichia coli K-12 Strain MG1655: B2166. (313 aa)
nrdARibonucleoside diphosphate reductase 1, alpha subunit, B1; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. (761 aa)
nrdBRibonucleoside diphosphage reductase 1, beta subunit, B2; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis. (376 aa)
yfbRPutative alpha helix protein; Catalyzes the strictly specific dephosphorylation of 2'- deoxyribonucleoside 5'-monophosphates. (199 aa)
uppUracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. (217 aa)
ndkNucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. (143 aa)
nrdERibonucleoside-diphosphate reductase 2, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. (714 aa)
nrdFRibonucleoside-diphosphate reductase 2, beta chain; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides; Belongs to the ribonucleoside diphosphate reductase small chain family. (319 aa)
surESurvival protein; 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. (253 aa)
pyrGCTP synthetase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. (545 aa)
mazGOrf, hypothetical protein; Involved in the regulation of bacterial cell survival under conditions of nutritional stress. Regulates the MazE-MazF toxin- antitoxin (TA) system that 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 (By similarity); Belongs to the nucleoside triphosphate py [...] (263 aa)
ygdHOrf, hypothetical protein; Catalyzes the hydrolysis of the N-glycosidic bond of diverse pyrimidine and purine nucleotide 5'-monophosphates, to form ribose 5- phosphate and the corresponding free base. Can use AMP, GMP, IMP, CMP, dTMP and UMP as substrates. Cannot catalyze the reverse reactions. May contribute to nucleoside pool homeostasis by degrading excess nucleotides and feeding back the ribose moiety to catabolism. Belongs to the LOG family. (454 aa)
thyAThymidylate synthetase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily. (264 aa)
hyuAOrf, hypothetical protein; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown. (465 aa)
yrfGPutative phosphatase; Residues 1 to 237 of 237 are 99.57 pct identical to residues 1 to 237 of 237 from Escherichia coli K-12 Strain MG1655: B3399. (237 aa)
dutDeoxyuridinetriphosphatase; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. (151 aa)
pyrEOrotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). (213 aa)
udpUridine phosphorylase; Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. Belongs to the PNP/UDP phosphorylase family. (253 aa)
cpdB2':3'-cyclic-nucleotide 2'-phosphodiesterase; Residues 1 to 647 of 647 are 99.38 pct identical to residues 1 to 647 of 647 from Escherichia coli K-12 Strain MG1655: B4213; Belongs to the 5'-nucleotidase family. (647 aa)
nrdDAnaerobic ribonucleoside-triphosphate reductase; Residues 1 to 712 of 712 are 99.85 pct identical to residues 1 to 712 of 712 from Escherichia coli K-12 Strain MG1655: B4238. (712 aa)
pyrIAspartate carbamoyltransferase, regulatory subunit; Involved in allosteric regulation of aspartate carbamoyltransferase. (153 aa)
pyrBAspartate carbamoyltransferase, catalytic subunit; Residues 1 to 311 of 311 are 100.00 pct identical to residues 1 to 311 of 311 from Escherichia coli K-12 Strain MG1655: B4245; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. (311 aa)
yjjGPutative 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 t [...] (225 aa)
deoAThymidine phosphorylase; The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. (440 aa)
deoDPurine-nucleoside phosphorylase; Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules; Belongs to the PNP/UDP phosphorylase family. (239 aa)
Your Current Organism:
Escherichia coli O157H7 EDL933
NCBI taxonomy Id: 155864
Other names: E. coli O157:H7 str. EDL933, Escherichia coli O157:H7 EDL933, Escherichia coli O157:H7 str. EDL933, Escherichia coli O157:H7 strain EDL933
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