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Database: UniProt
Entry: Q7NKL3
LinkDB: Q7NKL3
Original site: Q7NKL3 
ID   QUEG_GLOVI              Reviewed;         319 AA.
AC   Q7NKL3;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   10-APR-2019, entry version 100.
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=gll1464;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales;
OC   Gloeobacteraceae; Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(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; BA000045; BAC89405.1; -; Genomic_DNA.
DR   RefSeq; NP_924410.1; NC_005125.1.
DR   RefSeq; WP_011141464.1; NC_005125.1.
DR   SMR; Q7NKL3; -.
DR   STRING; 251221.35212029; -.
DR   EnsemblBacteria; BAC89405; BAC89405; BAC89405.
DR   GeneID; 2598642; -.
DR   KEGG; gvi:gll1464; -.
DR   PATRIC; fig|251221.4.peg.1496; -.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   HOGENOM; HOG000272644; -.
DR   InParanoid; Q7NKL3; -.
DR   KO; K18979; -.
DR   OMA; ICDTDLS; -.
DR   OrthoDB; 1478472at2; -.
DR   PhylomeDB; Q7NKL3; -.
DR   BioCyc; GVIO251221:G1G3K-1484-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000557; 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; 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    319       Epoxyqueuosine reductase.
FT                                /FTId=PRO_0000416072.
FT   DOMAIN      173    202       4Fe-4S ferredoxin-type.
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       236    236       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       239    239       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       243    243       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   319 AA;  34806 MW;  BC2D8254709A608C CRC64;
     MAPTAAQIKS RARALGFHKV GIARADALDG EAAERLGGWL AAGYAGEMRW MHDPRRRDIQ
     QVLPGVRSVI CVALSYNTAQ GEPAPGQARI SRYALGRDYH KVLGKPLKEL ARWIEASDPG
     CRAVAYVDTG PVQEKAWAEA AGLGWIGKNA CLITLEYGSW VFLGEILTTL DLEANDPHPN
     YCGTCTRCLS ACPTAALVEP AVVDARKCLA YHTIENRAPE LPEAIAEHQH GWVVGCDLCQ
     TCCPFNLRAE RWGRYSEVAD FAPRDPWNEI TLDQLADLSD AEFERWSEGS AIRRVKASGL
     RRNARSALGA SGDSLAQAH
//
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