STRINGSTRING
miaB miaB ileS ileS rluA rluA gluQ gluQ tilS tilS queA queA tgt tgt thiI thiI smtA smtA rlmL rlmL mnmA mnmA tsaB tsaB cmoA cmoA cmoB cmoB yegQ yegQ folE folE rsuA rsuA truA truA mnmC mnmC tmcA tmcA trmJ trmJ tadA tadA trmN trmN trmD trmD tcdA tcdA trmI trmI tsaD tsaD yhbO yhbO truB truB tsaC tsaC trmH trmH mnmE mnmE mnmG mnmG rluF rluF dusA dusA tsaE tsaE miaA miaA
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
miaBtRNA-i(6)A37 methylthiotransferase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (474 aa)
ileSisoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). (938 aa)
rluADual-specificity RNA pseudouridine synthase RluA; Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem and loop of transfer RNAs. (219 aa)
gluQglutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in position 34 of the tRNA(Asp), the wobble position of the QUC anticodon. Does not transfer glutamate to either tRNA(Glu) or tRNA(Gln). The incapacity of the glutamylated tRNA(Asp) to bind elongation factor Tu suggests that it is not involved in ribosomal protein biosynthesis. (308 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)
thiItRNA s(4)U8 sulfurtransferase; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. Belongs to the ThiI family. (482 aa)
smtAPutative S-adenosyl-L-methionine-dependent methyltransferase; Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs. Four tRNAs (tRNA(Ala1), tRNA(Ser1), tRNA(Pro3) and tRNA(Thr4)) are fully modified with mcmo5U in stationary-phase E.coli. Also present at low frequency in tRNA(Leu3) and tRNA(Val1). (261 aa)
rlmL23S rRNA m(2)G2445 and m(7)G2069 methyltransferases, SAM-dependent; Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Methylation occurs before assembly of 23S rRNA into 50S subunits. Belongs to the methyltransferase superfamily. RlmKL family. (702 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)
tsaBtRNA(ANN) t(6)A37 threonylcarbamoyladenosine modification protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, can act as a protease that specifically degrades TsaD in vitro; therefore TsaB may po [...] (231 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)
yegQPutative peptidase; Belongs to the peptidase U32 family. (453 aa)
folEGTP cyclohydrolase I; Protein involved in folic acid biosynthetic process; Belongs to the GTP cyclohydrolase I family. (222 aa)
rsuA16S rRNA pseudouridine(516) synthase; Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA; Belongs to the pseudouridine synthase RsuA family. (231 aa)
truAtRNA pseudouridine(38-40) synthase; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. (270 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)
tmcAElongator methionine tRNA (ac4C34) acetyltransferase; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). It recognizes the wobble base of tRNA(Met), thus distinguishing between tRNA(Met) and the structurally similar tRNA(Ile2). (671 aa)
trmJtRNA mC32,mU32 2'-O-methyltransferase, SAM-dependent; Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. Can also methylate adenosine or guanosine, even though these nucleosides are rare or absent at position 32 in the anticodon loop of tRNA. (246 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)
trmNtRNA1(Val) (adenine(37)-N6)-methyltransferase; Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC); Belongs to the methyltransferase superfamily. tRNA (adenine-N(6)-)-methyltransferase family. (245 aa)
trmDtRNA m(1)G37 methyltransferase, SAM-dependent; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. (255 aa)
tcdAtRNA threonylcarbamoyladenosine dehydratase; Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine. TcdA is also part of a sulfur transfer pathway; is able to accept sulfur from CsdA directly in vitro, but CsdE might act as the sulfur donor in vivo; Belongs to the HesA/MoeB/ThiF family. (268 aa)
trmItRNA m(7)G46 methyltransferase, SAM-dependent; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family. (239 aa)
tsaDtRNA(ANN) t(6)A37 threonylcarbamoyladenosine modification protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. May also be involved in the metabolism of glycated proteins, but does not show sialoglycoprotease activity against glycophorin A. (337 aa)
yhbOStress-resistance protein; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, glyceraldehyde-3-phospha [...] (172 aa)
truBtRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. (314 aa)
tsaCThreonylcarbamoyl-AMP synthase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Is also able to catalyze the reverse reaction in vitro, i.e. the formation of ATP from TC-AMP and PPi. Shows higher affinity for the full-length tRNA(Thr) lacking only the t(6)A37 modification than for its fully modified counterpart. Could also [...] (190 aa)
trmHtRNA mG18-2'-O-methyltransferase, SAM-dependent; Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. Type II methylase, which methylates only a subset of tRNA species; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. (229 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)
rluF23S rRNA pseudouridine(2604) synthase; Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-2604 in 23S ribosomal RNA and from uracil-35 in the anticodon of tRNA(Tyr). Can, to a small extent, also react with uracil-2605. Belongs to the pseudouridine synthase RsuA family. (290 aa)
dusAtRNA-dihydrouridine synthase A; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs; Belongs to the Dus family. DusA subfamily. (345 aa)
tsaEtRNA(ANN) t(6)A37 threonylcarbamoyladenosine modification protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. Displays ATPase activity in vitro. (153 aa)
miaADelta(2)-isopentenylpyrophosphate tRNA-adenosine transferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family. (316 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
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.