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Database: UniProt
Entry: P39288
LinkDB: P39288
Original site: P39288 
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   10-APR-2019, entry version 140.
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; Proteobacteria; 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.,
RA   Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT   region 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.,
RA   Mau B., 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
RT   MG1655 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
CC       queuosine (Q), which is a hypermodified base found in the wobble
CC       positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
CC       {ECO:0000255|HAMAP-Rule:MF_00916}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + epoxyqueuosine(34) in tRNA = A + H2O +
CC         queuosine(34) in tRNA; Xref=Rhea:RHEA:32159, Rhea:RHEA-
CC         COMP:10345, Rhea:RHEA-COMP:10346, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:82831,
CC         ChEBI:CHEBI:82834; EC=1.17.99.6; Evidence={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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00916}.
CC   -!- DISRUPTION PHENOTYPE: RNA from mutants accumulates epoxyqueuosine
CC       and lacks queuosine. {ECO:0000269|PubMed:21502530}.
CC   -!- SIMILARITY: Belongs to the QueG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00916}.
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_LN832404.1.
DR   ProteinModelPortal; P39288; -.
DR   SMR; P39288; -.
DR   BioGrid; 4262703; 4.
DR   IntAct; P39288; 2.
DR   STRING; 511145.b4166; -.
DR   PaxDb; P39288; -.
DR   PRIDE; P39288; -.
DR   EnsemblBacteria; AAC77123; AAC77123; b4166.
DR   EnsemblBacteria; BAE78167; BAE78167; BAE78167.
DR   GeneID; 948686; -.
DR   KEGG; ecj:JW4124; -.
DR   KEGG; eco:b4166; -.
DR   PATRIC; fig|1411691.4.peg.2535; -.
DR   EchoBASE; EB2374; -.
DR   EcoGene; EG12481; queG.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   HOGENOM; HOG000272643; -.
DR   InParanoid; P39288; -.
DR   KO; K18979; -.
DR   PhylomeDB; P39288; -.
DR   BioCyc; EcoCyc:G7843-MONOMER; -.
DR   BioCyc; ECOL316407:JW4124-MONOMER; -.
DR   BioCyc; MetaCyc:G7843-MONOMER; -.
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   HAMAP; MF_00916; QueG; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR013542; DUF1730.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR004453; QueG.
DR   PANTHER; PTHR30002; PTHR30002; 1.
DR   Pfam; PF08331; DUF1730; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   TIGRFAMs; TIGR00276; TIGR00276; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Queuosine biosynthesis;
KW   Reference proteome; tRNA processing.
FT   CHAIN         1    379       Epoxyqueuosine reductase.
FT                                /FTId=PRO_0000159304.
FT   DOMAIN      181    213       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       193    193       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       196    196       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       199    199       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       203    203       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       246    246       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       249    249       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       253    253       Iron-sulfur 1 (4Fe-4S).
FT                                {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
//
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