ID QUEG_ECOLI Reviewed; 379 AA.
AC P39288; Q2M6D9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 24-JAN-2024, entry version 163.
DE RecName: Full=Epoxyqueuosine reductase {ECO:0000255|HAMAP-Rule:MF_00916};
DE EC=1.17.99.6 {ECO:0000255|HAMAP-Rule:MF_00916};
DE AltName: Full=Queuosine biosynthesis protein QueG {ECO:0000255|HAMAP-Rule:MF_00916};
GN Name=queG {ECO:0000255|HAMAP-Rule:MF_00916}; Synonyms=yjeS;
GN OrderedLocusNames=b4166, JW4124;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
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 [3]
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 [4]
RP DISRUPTION PHENOTYPE, PATHWAY, AND GENE NAME.
RC STRAIN=K12;
RX PubMed=21502530; DOI=10.1073/pnas.1018636108;
RA Miles Z.D., McCarty R.M., Molnar G., Bandarian V.;
RT "Discovery of epoxyqueuosine (oQ) reductase reveals parallels between
RT halorespiration and tRNA modification.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7368-7372(2011).
CC -!- FUNCTION: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine
CC (Q), which is a hypermodified base found in the wobble positions of
CC tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr). {ECO:0000255|HAMAP-
CC Rule:MF_00916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in
CC tRNA; Xref=Rhea:RHEA:32159, Rhea:RHEA-COMP:18571, Rhea:RHEA-
CC COMP:18582, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:194431, ChEBI:CHEBI:194443; EC=1.17.99.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00916};
CC -!- COFACTOR:
CC Name=cob(II)alamin; Xref=ChEBI:CHEBI:16304;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00916};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00916};
CC Note=Binds 2 [4Fe-4S] clusters per monomer. {ECO:0000255|HAMAP-
CC Rule:MF_00916};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00916, ECO:0000269|PubMed:21502530}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00916}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00916}.
CC -!- DISRUPTION PHENOTYPE: RNA from mutants accumulates epoxyqueuosine and
CC lacks queuosine. {ECO:0000269|PubMed:21502530}.
CC -!- SIMILARITY: Belongs to the QueG family. {ECO:0000255|HAMAP-
CC Rule:MF_00916}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U14003; AAA97062.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77123.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78167.1; -; Genomic_DNA.
DR PIR; S56391; S56391.
DR RefSeq; NP_418587.1; NC_000913.3.
DR RefSeq; WP_001294219.1; NZ_STEB01000013.1.
DR AlphaFoldDB; P39288; -.
DR SMR; P39288; -.
DR BioGRID; 4262703; 4.
DR IntAct; P39288; 2.
DR STRING; 511145.b4166; -.
DR PaxDb; 511145-b4166; -.
DR EnsemblBacteria; AAC77123; AAC77123; b4166.
DR GeneID; 75202400; -.
DR GeneID; 948686; -.
DR KEGG; ecj:JW4124; -.
DR KEGG; eco:b4166; -.
DR PATRIC; fig|1411691.4.peg.2535; -.
DR EchoBASE; EB2374; -.
DR eggNOG; COG1600; Bacteria.
DR HOGENOM; CLU_030790_0_1_6; -.
DR InParanoid; P39288; -.
DR OMA; FPAPYQL; -.
DR OrthoDB; 9784571at2; -.
DR PhylomeDB; P39288; -.
DR BioCyc; EcoCyc:G7843-MONOMER; -.
DR BioCyc; MetaCyc:G7843-MONOMER; -.
DR BRENDA; 1.17.99.6; 2026.
DR UniPathway; UPA00392; -.
DR PRO; PR:P39288; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0052693; F:epoxyqueuosine reductase activity; IMP:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008616; P:queuosine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.20; -; 1.
DR HAMAP; MF_00916; QueG; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004453; QueG.
DR InterPro; IPR013542; QueG_DUF1730.
DR NCBIfam; TIGR00276; tRNA epoxyqueuosine(34) reductase QueG; 1.
DR PANTHER; PTHR30002; EPOXYQUEUOSINE REDUCTASE; 1.
DR PANTHER; PTHR30002:SF4; EPOXYQUEUOSINE REDUCTASE; 1.
DR Pfam; PF13484; Fer4_16; 1.
DR Pfam; PF08331; QueG_DUF1730; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Queuosine biosynthesis; Reference proteome; tRNA processing.
FT CHAIN 1..379
FT /note="Epoxyqueuosine reductase"
FT /id="PRO_0000159304"
FT DOMAIN 181..213
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT ACT_SITE 139
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 203
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 219
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 246
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 249
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 253
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
SQ SEQUENCE 379 AA; 43073 MW; E0440A59BCD753F7 CRC64;
MSEPLDLNQL AQKIKQWGLE LGFQQVGITD TDLSESEPKL QAWLDKQYHG EMDWMARHGM
LRARPHELLP GTLRVISVRM NYLPANAAFA STLKNPKLGY VSRYALGRDY HKLLRNRLKK
LGEMIQQHCV SLNFRPFVDS APILERPLAE KAGLGWTGKH SLILNREAGS FFFLGELLVD
IPLPVDQPVE EGCGKCVACM TICPTGAIVE PYTVDARRCI SYLTIELEGA IPEELRPLMG
NRIYGCDDCQ LICPWNRYSQ LTTEEDFSPR KPLHAPELIE LFAWSEEKFL KVTEGSAIRR
IGHLRWLRNI AVALGNAPWD ETILTALESR KGEHPLLDEH IAWAIAQQIE RRNACIVEVQ
LPKKQRLVRV IEKGLPRDA
//
