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Database: UniProt
Entry: A0A0U1QLE6_9BACL
LinkDB: A0A0U1QLE6_9BACL
Original site: A0A0U1QLE6_9BACL 
ID   A0A0U1QLE6_9BACL        Unreviewed;       384 AA.
AC   A0A0U1QLE6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
DE   RecName: Full=Epoxyqueuosine reductase {ECO:0000256|HAMAP-Rule:MF_00916};
DE            EC=1.17.99.6 {ECO:0000256|HAMAP-Rule:MF_00916};
DE   AltName: Full=Queuosine biosynthesis protein QueG {ECO:0000256|HAMAP-Rule:MF_00916};
GN   Name=queG {ECO:0000256|HAMAP-Rule:MF_00916};
GN   ORFNames=SINU_12575 {ECO:0000313|EMBL:KLI01635.1};
OS   Sporolactobacillus inulinus CASD.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   Sporolactobacillus.
OX   NCBI_TaxID=1069536 {ECO:0000313|EMBL:KLI01635.1, ECO:0000313|Proteomes:UP000035553};
RN   [1] {ECO:0000313|EMBL:KLI01635.1, ECO:0000313|Proteomes:UP000035553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CASD {ECO:0000313|EMBL:KLI01635.1,
RC   ECO:0000313|Proteomes:UP000035553};
RX   PubMed=21952540; DOI=10.1128/JB.05934-11;
RA   Yu B., Su F., Wang L., Xu K., Zhao B., Xu P.;
RT   "Draft genome sequence of Sporolactobacillus inulinus strain CASD, an
RT   efficient D-lactic acid-producing bacterium with high-concentration
RT   lactate tolerance capability.";
RL   J. Bacteriol. 193:5864-5865(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:0000256|HAMAP-Rule:MF_00916}.
CC   -!- CATALYTIC ACTIVITY: Queuosine(34) in tRNA + acceptor + H(2)O =
CC       epoxyqueuosine(34) in tRNA + reduced acceptor. {ECO:0000256|HAMAP-
CC       Rule:MF_00916}.
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00916}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00916}.
CC   -!- SIMILARITY: Belongs to the QueG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00916}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KLI01635.1}.
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DR   EMBL; AFVQ02000182; KLI01635.1; -; Genomic_DNA.
DR   EnsemblBacteria; KLI01635; KLI01635; SINU_12575.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000035553; Unassembled WGS sequence.
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; IPR016024; ARM-type_fold.
DR   InterPro; IPR013542; DUF1730.
DR   InterPro; IPR004453; QueG.
DR   PANTHER; PTHR30002; PTHR30002; 1.
DR   Pfam; PF08331; DUF1730; 1.
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 {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035553};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035553};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   DOMAIN      178    208       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL       188    188       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       191    191       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       194    194       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       198    198       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       240    240       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       243    243       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       247    247       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   384 AA;  43604 MW;  13B2DF925BB2E6EF CRC64;
     MDFQELKEQL IRYSKEIGVD KIGFTTADPF TELKARLYRQ RELGYQSGFE EKDIEKRTEP
     SLLMDGVQSI VSIAMAYPKK MAERPANTKG HRRGAFARVS WGQDYHTILR DRMQKLGEFL
     VETVPGATFK SMVDTGELSD RAVAERAGIG WAGKSTNLIT KEFGSYVYLG EMLTNIPFPP
     DKPATDLCGD CTICIDHCPT GALVQGGQLN SQKCIAYLTQ TKQELPEEYK KAIGNRLYGC
     DMCQQVCPYN RDVDSHFHEE MEPDPELAHP LLTPLLTLSN RAFKETFGDV SGSWRGKKPI
     QRNAIVALGN YKEVAAALEL LRLLHDDPRP VIRRTVTWAL QQMWDRLEPD MRAHMIQSFE
     DLLAKEEDEK VHQWIKAKLD AEEG
//
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