QUEA_ECOLI
ID QUEA_ECOLI Reviewed; 356 AA.
AC P0A7F9; P21516; Q2MC21;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase;
DE EC=2.4.99.17;
DE AltName: Full=Queuosine biosynthesis protein QueA;
GN Name=queA; OrderedLocusNames=b0405, JW0395;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1706703; DOI=10.1128/jb.173.7.2256-2264.1991;
RA Reuter K., Slany R., Ullrich F., Kersten H.;
RT "Structure and organization of Escherichia coli genes involved in
RT biosynthesis of the deazaguanine derivative queuine, a nutrient factor for
RT eukaryotes.";
RL J. Bacteriol. 173:2256-2264(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8347586; DOI=10.1021/bi00081a028;
RA Slany R.K., Boesl M., Crain P.F., Kersten H.;
RT "A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is
RT the precursor of the cyclopentenediol moiety of the tRNA wobble base
RT queuine.";
RL Biochemistry 32:7811-7817(1993).
RN [6]
RP CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RC STRAIN=K12;
RX PubMed=7849103; DOI=10.1016/0300-9084(94)90113-9;
RA Slany R.K., Boesl M., Kersten H.;
RT "Transfer and isomerization of the ribose moiety of AdoMet during the
RT biosynthesis of queuosine tRNAs, a new unique reaction catalyzed by the
RT QueA protein from Escherichia coli.";
RL Biochimie 76:389-393(1994).
RN [7]
RP KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITORS.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=12731872; DOI=10.1021/bi034197u;
RA Van Lanen S.G., Iwata-Reuyl D.;
RT "Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA
RT ribosyltransferase-isomerase (QueA).";
RL Biochemistry 42:5312-5320(2003).
CC -!- FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet to the
CC 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give
CC epoxyqueuosine (oQ-tRNA).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-
CC methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-
CC methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342, Rhea:RHEA-
CC COMP:10346, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:82833, ChEBI:CHEBI:82834;
CC EC=2.4.99.17; Evidence={ECO:0000269|PubMed:7849103};
CC -!- ACTIVITY REGULATION: Inhibited by S-adenosylhomocysteine,
CC adenosylornithine and products.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=98 uM for S-adenosylmethionine {ECO:0000269|PubMed:12731872};
CC KM=1.9 uM for 7-(aminomethyl)-7-deazaguanosine
CC {ECO:0000269|PubMed:12731872};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: This reaction follows a completely ordered sequential
CC bi-ter kinetic mechanism, with binding of preQ1-tRNATyr followed by
CC AdoMet to form the ternary complex. Products are then released in the
CC following order: adenine, methionine, and oQ-tRNATyr.
CC -!- SIMILARITY: Belongs to the QueA family. {ECO:0000305}.
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DR EMBL; M37702; AAA16114.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40161.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73508.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76185.1; -; Genomic_DNA.
DR PIR; B38530; B38530.
DR RefSeq; NP_414939.1; NC_000913.3.
DR RefSeq; WP_001266503.1; NZ_STEB01000007.1.
DR AlphaFoldDB; P0A7F9; -.
DR SMR; P0A7F9; -.
DR BioGRID; 4262056; 62.
DR DIP; DIP-47972N; -.
DR IntAct; P0A7F9; 5.
DR STRING; 511145.b0405; -.
DR jPOST; P0A7F9; -.
DR PaxDb; P0A7F9; -.
DR PRIDE; P0A7F9; -.
DR EnsemblBacteria; AAC73508; AAC73508; b0405.
DR EnsemblBacteria; BAE76185; BAE76185; BAE76185.
DR GeneID; 66671296; -.
DR GeneID; 944905; -.
DR KEGG; ecj:JW0395; -.
DR KEGG; eco:b0405; -.
DR PATRIC; fig|1411691.4.peg.1872; -.
DR EchoBASE; EB0805; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_0_6; -.
DR InParanoid; P0A7F9; -.
DR OMA; YSYGDGM; -.
DR PhylomeDB; P0A7F9; -.
DR BioCyc; EcoCyc:EG10812-MON; -.
DR BioCyc; MetaCyc:EG10812-MON; -.
DR SABIO-RK; P0A7F9; -.
DR UniPathway; UPA00392; -.
DR PRO; PR:P0A7F9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IDA:EcoCyc.
DR GO; GO:0008616; P:queuosine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR GO; GO:0002099; P:tRNA wobble guanine modification; IMP:EcoCyc.
DR Gene3D; 2.40.10.240; -; 1.
DR Gene3D; 3.40.1780.10; -; 1.
DR HAMAP; MF_00113; QueA; 1.
DR InterPro; IPR003699; QueA.
DR InterPro; IPR042118; QueA_dom1.
DR InterPro; IPR042119; QueA_dom2.
DR InterPro; IPR036100; QueA_sf.
DR PANTHER; PTHR30307; PTHR30307; 1.
DR Pfam; PF02547; Queuosine_synth; 1.
DR SUPFAM; SSF111337; SSF111337; 1.
DR TIGRFAMs; TIGR00113; queA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Queuosine biosynthesis; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..356
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_0000165400"
SQ SEQUENCE 356 AA; 39431 MW; 47F7F0090812DCF3 CRC64;
MRVTDFSFEL PESLIAHYPM PERSSCRLLS LDGPTGALTH GTFTDLLDKL NPGDLLVFNN
TRVIPARLFG RKASGGKIEV LVERMLDDKR ILAHIRASKA PKPGAELLLG DDESINATMT
ARHGALFEVE FNDERSVLDI LNSIGHMPLP PYIDRPDEDA DRELYQTVYS EKPGAVAAPT
AGLHFDEPLL EKLRAKGVEM AFVTLHVGAG TFQPVRVDTI EDHIMHSEYA EVPQDVVDAV
LAAKARGNRV IAVGTTSVRS LESAAQAAKN DLIEPFFDDT QIFIYPGFQY KVVDALVTNF
HLPESTLIML VSAFAGYQHT MNAYKAAVEE KYRFFSYGDA MFITYNPQAI NERVGE
