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Database: UniProt
Entry: Q834R1
LinkDB: Q834R1
Original site: Q834R1 
ID   QUEG_ENTFA              Reviewed;         389 AA.
AC   Q834R1;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   10-APR-2019, entry version 106.
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};
GN   OrderedLocusNames=EF_1578;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
RA   Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
RA   Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
RA   Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant
RT   Enterococcus faecalis.";
RL   Science 299:2071-2074(2003).
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00916}.
CC   -!- SIMILARITY: Belongs to the QueG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00916}.
DR   EMBL; AE016830; AAO81365.1; -; Genomic_DNA.
DR   RefSeq; NP_815295.1; NC_004668.1.
DR   RefSeq; WP_002382325.1; NZ_KE136528.1.
DR   ProteinModelPortal; Q834R1; -.
DR   SMR; Q834R1; -.
DR   STRING; 226185.EF_1578; -.
DR   DNASU; 1200478; -.
DR   EnsemblBacteria; AAO81365; AAO81365; EF_1578.
DR   GeneID; 1200478; -.
DR   KEGG; efa:EF1578; -.
DR   PATRIC; fig|226185.45.peg.1927; -.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   KO; K18979; -.
DR   OMA; ICDTDLS; -.
DR   BioCyc; EFAE226185:G1G0C-1564-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001415; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.10.10; -; 1.
DR   HAMAP; MF_00916; QueG; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013542; DUF1730.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   InterPro; IPR004453; QueG.
DR   PANTHER; PTHR30002; PTHR30002; 1.
DR   Pfam; PF08331; DUF1730; 1.
DR   SMART; SM00567; EZ_HEAT; 2.
DR   SUPFAM; SSF48371; SSF48371; 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    389       Epoxyqueuosine reductase.
FT                                /FTId=PRO_0000416069.
FT   DOMAIN      181    210       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   REPEAT      303    328       HEAT-like PBS-type.
FT   METAL       190    190       Iron-sulfur 1 (4Fe-4S).
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       200    200       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       242    242       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       245    245       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       249    249       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   389 AA;  44195 MW;  510739B350D6ED94 CRC64;
     MPTLKEKIIQ ESQRLGIDKI GFTHAEPFIE LEDSLHEQRE RGYNSGFEHQ NVEERIYPEK
     TFEHPKSIIS IALAYPTKAQ EKMPRDEKRG QFARASWGID YHHILQDRLQ KLIAFIEEQA
     ATEAEKEHWR FRPQVDTGEY VDTAVAQRAG LGFIGKNGLL ITEEFGSFVY LGEVTTNIQF
     EPDEPVPNGC GDCTRCITGC PTGALLGDGR MNAQKCLSYQ TQTKGMMPED YRKKMRNVIY
     GCDICQLVCP YNKGKDFHFH EEMEPKIEEV YPKLAPLLTI SNKEFKQQFG HLAGSWRGKK
     PLQRNALIAL ANLGGREAIP QIILCLNDQR PVIRGTAAWS LGQLAKREPE QSLEALNYLL
     SVETEEEVIE EAQKAIHLLT SKKGSRSTE
//
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