(data stored in ACNUC7421 zone)

SWISSPROT: C5BDM5_EDWI9

ID   C5BDM5_EDWI9            Unreviewed;       379 AA.
AC   C5BDM5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
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   OrderedLocusNames=NT01EI_0403 {ECO:0000313|EMBL:ACR67641.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67641.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001600; ACR67641.1; -; Genomic_DNA.
DR   RefSeq; WP_015869847.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0403; -.
DR   EnsemblBacteria; ACR67641; ACR67641; NT01EI_0403.
DR   GeneID; 7959004; -.
DR   KEGG; eic:NT01EI_0403; -.
DR   PATRIC; fig|634503.3.peg.363; -.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   HOGENOM; HOG000272643; -.
DR   KO; K18979; -.
DR   OMA; VDGSKCI; -.
DR   OrthoDB; POG091H01VA; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001485; 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-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP.
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:SF6; PTHR30002:SF6; 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;
DR   PRODOM; C5BDM5.
DR   SWISS-2DPAGE; C5BDM5.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
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:UP000001485};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   DOMAIN      181    213       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL       193    193       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       196    196       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       199    199       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       203    203       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       246    246       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       249    249       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       253    253       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   379 AA;  42320 MW;  3E701F8932A4D7EC CRC64;
     MTHPLDLHQL AQHIKQWGLS LGFQQVGIGD TDLRAEEAPL QAWLDSGYHG DMAWMARHGM
     MRARPAELLP GTLRVISVRM NYLPPSAAFA STLKDPTLGY ISRYALGRDY HKVLRARLKK
     LGEMIQAYCG ELRFRPFVDS APLLERPLAA KAGLGWTGKH SLLLNPQAGS WFFLGELLID
     LPLPVDTPQT AQCGRCVACI TTCPTDAIVA PYKVDARRCI SYLTIELEGA IPEALRPLLG
     NRIYGCDDCQ MICPWNRLAP LSEEADFLPR AALHAPPLTI LFAWDETTFL RMTEGSPIRR
     IGYQRWLRNL SVALGNAPYD AHIVTLLQQR LGVSALLDEH IHWALAQQLQ KRAAQAVEVV
     SSQQRRLIRA VEKGLPRDA
//

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