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queG queG mnmH mnmH tilS tilS queA queA tgt tgt queC queC mnmA mnmA cmoA cmoA cmoB cmoB folE folE mnmC mnmC tadA tadA queD queD queE queE queF queF trmL trmL mnmE mnmE mnmG mnmG rplA rplA rpoB rpoB
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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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query proteins and first shell of interactors
white nodes:
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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experimentally determined
Predicted Interactions
gene neighborhood
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textmining
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queGEpoxyqueuosine reductase, cobalamine-stimulated; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr). (379 aa)
mnmHtRNA 2-selenouridine synthase; Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U) and subsequent selenation of the latter derivative to 2-selenouridine (Se2U) in the tRNA chain. (364 aa)
tilStRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This enzyme is essential for viability. (432 aa)
queAS-adenosylmethionine:tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA); Belongs to the QueA family. (356 aa)
tgttRNA-guanine transglycosylase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the [...] (375 aa)
queC7-cyano-7-deazaguanine (preQ0) synthase; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). (231 aa)
mnmAtRNA(Gln,Lys,Glu) U34 2-thiouridylase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs. (368 aa)
cmoAcarboxy-SAM synthase; Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM); Belongs to the class I-like SAM-binding methyltransferase superfamily. Cx-SAM synthase family. (247 aa)
cmoBtRNA (cmo5U34)-carboxymethyltransferase, carboxy-SAM-dependent; Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L- methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5- carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. Can also catalyze the SAM-dependent methylation of ho5U, with much lower efficiency. (323 aa)
folEGTP cyclohydrolase I; Protein involved in folic acid biosynthetic process; Belongs to the GTP cyclohydrolase I family. (222 aa)
mnmCtRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC; Catalyzes the last two steps in the biosynthesis of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34; In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family. (668 aa)
tadAtRNA-specific adenosine deaminase; Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2). Essential for cell viability. Belongs to the cytidine and deoxycytidylate deaminase family. (167 aa)
queD6-pyruvoyl tetrahydrobiopterin synthase (PTPS); Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. Can also convert 6-pyruvoyltetrahydropterin (PPH4) and sepiapterin to CPH4; these 2 compounds are probably intermediates in the reaction from H2NTP. (121 aa)
queE7-carboxy-7-deazaguanine synthase; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (223 aa)
queF7-cyano-7-deazaguanine reductase (NADPH-dependent); Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1), a late step in the queuosine pathway. Is highly specific for its natural substrate preQ0, since it cannot use various aliphatic, aromatic, benzylic and heterocyclic nitriles, such as acetonitrile, benzonitrile, benzylcyanide and 2-cyanopyrrole, although it can reduce the substrate analog 5-cyanopyrrolo[2,3-d]pyrimidin-4-one with lesser efficiency. Belongs to the GTP cyclohydrolase I family. QueF type 2 subfamily. (282 aa)
trmLtRNA Leu mC34,mU34 2'-O-methyltransferase, SAM-dependent; Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. Recognition of the target requires a pyridine at position 34 and N(6)-(isopentenyl)-2-methylthioadenosine at position 37. (157 aa)
mnmEtRNA U34 5-methylaminomethyl-2-thiouridine modification GTPase; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34. (454 aa)
mnmG5-methylaminomethyl-2-thiouridine modification at tRNA U34; NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. (629 aa)
rplA50S ribosomal subunit protein L1; One of the primary rRNA binding proteins, it binds very close to the 3'-end of the 23S rRNA. Forms part of the L1 stalk. It is often not seen in high-resolution crystal structures, but can be seen in cryo_EM and 3D reconstruction models. These indicate that the distal end of the stalk moves by approximately 20 angstroms. This stalk movement is thought to be coupled to movement of deacylated tRNA into and out of the E site, and thus to participate in tRNA translocation. Contacts the P and E site tRNAs. (234 aa)
rpoBRNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1342 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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