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mtn mtn dnaQ dnaQ mdfA mdfA focA focA putP putP narK narK chbC chbC napC napC napA napA nuoE nuoE yffB yffB xerD xerD php php arsR arsR nrfA nrfA
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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
Your Input:
mtn5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5- deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulati [...] (232 aa)
dnaQDNA polymerase III epsilon subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. Contacts both the beta sliding clamp (dnaN) and the polymerase subunit (dnaE), stabilizing their interaction. (243 aa)
mdfAMultidrug efflux system protein; Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracycline, puromycin, and to chemically unrelated, clinically important antibiotics such as chloramphenicol, erythromycin, and certain aminoglycosides and fluoroquinolones. Overexpression results in isopropyl-beta-D- thiogalactopyranoside (IPTG) exclusi [...] (410 aa)
focAFormate channel; Involved in the bidirectional transport of formate; Belongs to the FNT transporter (TC 2.A.44) family. (285 aa)
putPProline:sodium symporter; Catalyzes the sodium-dependent uptake of extracellular L- proline. This protein is also capable of using lithium as the transport cation. Also catalyzes the uptake of propionate. (502 aa)
narKNitrate/nitrite transporter; Catalyzes nitrate uptake, nitrite uptake and nitrite export across the cytoplasmic membrane. Functions as a nitrate/nitrite exchanger, and protons are probably not co-transported with the substrate. (463 aa)
chbCN,N'-diacetylchitobiose-specific enzyme IIC component of PTS; The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ChbABC PTS system is involved in the transport of the chitin disaccharide N,N'-diacetylchitobiose (GlcNAc2). Also able to use N,N',N''-triacetyl chitotriose (GlcNAc3). (452 aa)
napCQuinol dehydrogenase, electron source for NapAB; Mediates electron flow from quinones to the NapAB complex. (200 aa)
napANitrate reductase, periplasmic, large subunit; Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. (828 aa)
nuoENADH:ubiquinone oxidoreductase, chain E; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (166 aa)
yffBPutative ArsC family reductase; Belongs to the ArsC family. (118 aa)
xerDSite-specific tyrosine recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids at ColE1 xer (or cer) and pSC101 (or [...] (298 aa)
phpPhosphotriesterase homology protein; Its real enzymatic activity is not yet known. It was tested for general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities with the following substrates: p-nitrophenyl acetate, L-alanine nitroanilide, p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-nitrophenyl phosphate. No enzymatic activity was detected with any of these non-specific substrates. (292 aa)
arsRArsenical resistance operon transcriptional repressor; Transcriptional repressor for the arsEFG operon. ArsE is a trans-acting regulatory protein which controls its own expression. The repressive effect of ArsE is alleviated by oxyions of +III oxidation state of arsenic, antimony, and bismuth, as well as arsenate (As(V)) (By similarity). (117 aa)
nrfANitrite reductase, formate-dependent, cytochrome; Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Has very low activity toward hydroxylamine. Has even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH (By similarity). (478 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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