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Database: UniProt
Entry: Q8Y8H0
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Original site: Q8Y8H0 
ID   QUEG_LISMO              Reviewed;         379 AA.
AC   Q8Y8H0;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-DEC-2018, entry version 101.
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=lmo0934;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA   Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA   Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA   Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA   Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA   Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591977; CAC99012.1; -; Genomic_DNA.
DR   PIR; AF1191; AF1191.
DR   RefSeq; NP_464459.1; NC_003210.1.
DR   RefSeq; WP_010989619.1; NC_003210.1.
DR   ProteinModelPortal; Q8Y8H0; -.
DR   SMR; Q8Y8H0; -.
DR   STRING; 169963.lmo0934; -.
DR   PaxDb; Q8Y8H0; -.
DR   EnsemblBacteria; CAC99012; CAC99012; CAC99012.
DR   GeneID; 986642; -.
DR   KEGG; lmo:lmo0934; -.
DR   PATRIC; fig|169963.11.peg.961; -.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   HOGENOM; HOG000272645; -.
DR   KO; K18979; -.
DR   OMA; ICDTDLS; -.
DR   PhylomeDB; Q8Y8H0; -.
DR   BioCyc; LMON169963:LMO0934-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000817; 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; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
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; 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    379       Epoxyqueuosine reductase.
FT                                /FTId=PRO_0000416075.
FT   DOMAIN      184    214       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   REPEAT      307    332       HEAT-like PBS-type.
FT   METAL       194    194       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       197    197       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       200    200       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       204    204       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;  42770 MW;  CF4B039C5DCF0B24 CRC64;
     MVVKQKADYA ALKEELIAYA YEIGIQKIGF TTADPFLFLK ERLLEAEALD LFTGFEHPVI
     EERVYPELIF KEPQSIIAIA LAYPSKLKEA PVSKKGARRG VFARASWGID YHTVLREKLA
     LLETFLIERL PDVRMKSMVD TGELSDVAVA ERAGIGWRGK NTLLITPEYG SWVYLGEMIT
     NIPFEPDTPA SDLCGSCNQC VKACPTGSLL GEGKMNPKIC LSYLTQTKDF LDEKYREVLH
     NRLYGCDTCQ VVCPYNRGHD FHFHEEMEPD PELVRPELKP LLHISNRAFK EQFGDMAGSW
     RGKKPIQRNA IIILARYKDK TAVPDLIDCL QNDPRPVIRG TAGWALRKIG GRDAEEAVER
     ALQTEQDVQV LQELTAIPN
//
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