STRINGSTRING
carA carA carB carB pyrH pyrH yaiE yaiE codA codA udk udk dcd dcd tdk tdk pyrF pyrF ydfG ydfG tmk tmk pyrC pyrC rutA rutA rutB rutB rutC rutC rutD rutD rutE rutE rutF rutF pyrD pyrD cmk cmk cdd cdd yeiT yeiT yeiA yeiA yeiI yeiI rihB rihB yeiN yeiN yeiC yeiC nrdA nrdA nrdB nrdB yfbR yfbR upp upp ndk ndk nrdE nrdE nrdF nrdF surE surE CAR19167.1 CAR19167.1 udp udp pyrG pyrG mazG mazG ygdH ygdH thyA thyA hyuA hyuA yrfG yrfG dut dut pyrE pyrE CAR20333.1 CAR20333.1 yeiN-2 yeiN-2 CAR20336.1 CAR20336.1 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
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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carACarbamoyl phosphate synthetase small subunit, glutamine amidotransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the CarA family. (382 aa)
carBCarbamoyl-phosphate synthase large subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the CarB family. (1073 aa)
pyrHUridylate kinase; Catalyzes the reversible phosphorylation of UMP to UDP. (241 aa)
yaiEConserved 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)
codACytosine deaminase; Function experimentally demonstrated in the studied species; enzyme. (427 aa)
udkUridine/cytidine kinase; Function experimentally demonstrated in the studied species; enzyme. (213 aa)
dcd2'-deoxycytidine 5'-triphosphate deaminase; Catalyzes the deamination of dCTP to dUTP. (193 aa)
tdkThymidine kinase/deoxyuridine kinase; Function experimentally demonstrated in the studied species; enzyme. (205 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)
ydfGL-allo-threonine dehydrogenase, NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (248 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)
pyrCDihydro-orotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. (348 aa)
rutAMonooxygenase of the alternative pyrimidine degradation pathway; 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; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. (331 aa)
rutBEnzyme of the alternative pyrimidine degradation pathway; 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. (230 aa)
rutCEnzyme of the alternative pyrimidine degradation pathway; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. (128 aa)
rutDEnzyme of the alternative pyrimidine degradation pathway; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. (266 aa)
rutEOxidoreductase subunit of the alternative pyrimidine degradation pathway; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted; Belongs to the nitroreductase family. HadB/RutE subfamily. (196 aa)
rutFflavin:NADH oxidoreductase subunit of alternative pyrimidine degradation pathway; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. (164 aa)
pyrDDihydro-orotate oxidase, FMN-linked; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. (336 aa)
cmkCytidylate kinase; Function experimentally demonstrated in the studied species; enzyme. (227 aa)
cddCytidine/deoxycytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. (294 aa)
yeiTPutative Fe-S cluster containing oxidoreductase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (412 aa)
yeiAPutative oxidoreductase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (411 aa)
yeiIPutative kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (362 aa)
rihBRibonucleoside hydrolase 2; 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)
yeiNConserved 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; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (313 aa)
nrdARibonucleoside diphosphate reductase 1, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. (761 aa)
nrdBRibonucleoside diphosphate reductase 1, beta subunit, ferritin-like; Function experimentally demonstrated in the studied species; carrier. (376 aa)
yfbRDeoxyribonucleoside 5'-monophosphatase; 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. (208 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 subunit, ferritin-like; 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)
surEBroad 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. (253 aa)
CAR19167.1Putative phosphoesterase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the 5'-nucleotidase family. (519 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. (256 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)
mazGNucleoside triphosphate pyrophosphohydrolase; Function experimentally demonstrated in the studied species; enzyme. (263 aa)
ygdHConserved hypothetical protein; Homologs of previously reported genes of unknown function. (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. (264 aa)
hyuAD-stereospecific phenylhydantoinase; 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. (461 aa)
yrfGPutative hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (222 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)
CAR20333.1Putative carbohydrate kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (364 aa)
yeiN-2Conserved 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. (311 aa)
CAR20336.1Putative carbohydrate kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (320 aa)
cpdB2':3'-cyclic-nucleotide 2'-phosphodiesterase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the 5'-nucleotidase family. (647 aa)
nrdDAnaerobic ribonucleoside-triphosphate reductase; Function experimentally demonstrated in the studied species; enzyme. (712 aa)
pyrIAspartate carbamoyltransferase, regulatory subunit; Involved in allosteric regulation of aspartate carbamoyltransferase. (153 aa)
pyrBAspartate carbamoyltransferase, catalytic subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. (311 aa)
yjjGdUMP phosphatase; Function experimentally demonstrated in the studied species; enzyme. (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; Function experimentally demonstrated in the studied species; enzyme. (239 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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