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Database: UniProt
Entry: E4RUV9
LinkDB: E4RUV9
Original site: E4RUV9 
ID   QUEG_LEAB4              Reviewed;         302 AA.
AC   E4RUV9;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   16-JAN-2019, entry version 47.
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=Lbys_1262;
OS   Leadbetterella byssophila (strain DSM 17132 / KACC 11308 / 4M15).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Leadbetterella.
OX   NCBI_TaxID=649349;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17132 / KACC 11308 / 4M15;
RX   PubMed=21475582; DOI=10.4056/sigs.1413518;
RA   Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M.,
RA   Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA   Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Goker M., Tindall B.J., Detter J.C., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Leadbetterella byssophila type strain
RT   (4M15).";
RL   Stand. Genomic Sci. 4:2-12(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}.
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; CP002305; ADQ16982.1; -; Genomic_DNA.
DR   RefSeq; WP_013408032.1; NC_014655.1.
DR   SMR; E4RUV9; -.
DR   STRING; 649349.Lbys_1262; -.
DR   EnsemblBacteria; ADQ16982; ADQ16982; Lbys_1262.
DR   KEGG; lby:Lbys_1262; -.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   HOGENOM; HOG000272644; -.
DR   KO; K18979; -.
DR   OMA; ICDTDLS; -.
DR   OrthoDB; 1478472at2; -.
DR   BioCyc; LBYS649349:G1GOY-1268-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000007435; 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   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; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Queuosine biosynthesis;
KW   Reference proteome; Repeat; tRNA processing.
FT   CHAIN         1    302       Epoxyqueuosine reductase.
FT                                /FTId=PRO_0000416074.
FT   DOMAIN      170    202       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   DOMAIN      221    251       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       182    182       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       185    185       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       188    188       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       192    192       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       234    234       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       237    237       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       241    241       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   302 AA;  34760 MW;  2F7B67A4CE33D186 CRC64;
     MRDYSKEIKS WAAELGFDFC GISAADFLEE EAPRLERWLN RNYHGKMAYM ANHFDKRLDP
     RKLVDGAKSV VSLLLNYYPE EPLDASPYKI SKYAYGKDYH YVIKDKLKLL FERIQKEIGE
     VGGRIFVDSA PVMDKIWAKK AGLGWVGKNS NLINRKMGSF FFIAELILDL PLQADGPIRD
     YCGTCTACID ACPTDAITPY EVDGSKCISY LTIELKDQIP NEFKGKMENW IFGCDICQDV
     CPWNSFARPH STEEFYPNEN LKTFQDWDEI TSEIFSHLFK KSAVERTKLE GLKRNIAFVK
     EV
//
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