GenomeNet

Database: UniProt
Entry: Q81YT7
LinkDB: Q81YT7
Original site: Q81YT7 
ID   QUEG_BACAN              Reviewed;         380 AA.
AC   Q81YT7; E9RA89; E9RA90; Q6I3N8; Q6KXF1;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   13-FEB-2019, entry version 139.
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=BA_0545, GBAA_0545, BAS0514;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H.,
RA   Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D.,
RA   Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F.,
RA   Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C.,
RA   Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O.,
RA   Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to
RT   closely related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/JB.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) 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: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; AE016879; AAP24566.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT29642.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT52843.1; -; Genomic_DNA.
DR   RefSeq; NP_843080.1; NC_003997.3.
DR   RefSeq; WP_000345223.1; NZ_QPKQ01000007.1.
DR   RefSeq; YP_026792.1; NC_005945.1.
DR   ProteinModelPortal; Q81YT7; -.
DR   SMR; Q81YT7; -.
DR   STRING; 260799.BAS0514; -.
DR   PRIDE; Q81YT7; -.
DR   DNASU; 1087855; -.
DR   EnsemblBacteria; AAP24566; AAP24566; BA_0545.
DR   EnsemblBacteria; AAT29642; AAT29642; GBAA_0545.
DR   EnsemblBacteria; AAT52843; AAT52843; BAS0514.
DR   GeneID; 1087855; -.
DR   GeneID; 2848025; -.
DR   KEGG; ban:BA_0545; -.
DR   KEGG; banh:HYU01_02975; -.
DR   KEGG; bar:GBAA_0545; -.
DR   KEGG; bat:BAS0514; -.
DR   PATRIC; fig|198094.11.peg.543; -.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   HOGENOM; HOG000272645; -.
DR   KO; K18979; -.
DR   BioCyc; BANT260799:BAS0514-MONOMER; -.
DR   BioCyc; GCF_001654475:G1ETW-625-MONOMER; -.
DR   BioCyc; GCF_001683065:G1EXM-625-MONOMER; -.
DR   BioCyc; GCF_001683095:G1EXN-625-MONOMER; -.
DR   BioCyc; GCF_001683135:G1EXO-625-MONOMER; -.
DR   BioCyc; GCF_001683155:G1EXP-625-MONOMER; -.
DR   BioCyc; GCF_001683175:G1EXQ-625-MONOMER; -.
DR   BioCyc; GCF_001683195:G1EXR-625-MONOMER; -.
DR   BioCyc; GCF_001683215:G1EXS-625-MONOMER; -.
DR   BioCyc; GCF_001683235:G1EXT-625-MONOMER; -.
DR   BioCyc; GCF_001683255:G1EXU-625-MONOMER; -.
DR   BioCyc; GCF_001683275:G1EXV-625-MONOMER; -.
DR   BioCyc; GCF_001683295:G1EXW-625-MONOMER; -.
DR   BioCyc; GCF_001936375:G1FL6-623-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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   Gene3D; 1.25.10.10; -; 1.
DR   HAMAP; MF_00916; QueG; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011989; ARM-like.
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; 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    380       Epoxyqueuosine reductase.
FT                                /FTId=PRO_0000416064.
FT   DOMAIN      179    208       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   DOMAIN      226    258       4Fe-4S ferredoxin-type 2.
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       191    191       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       194    194       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
FT   METAL       198    198       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       240    240       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       243    243       Iron-sulfur 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00916}.
FT   METAL       247    247       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   380 AA;  42417 MW;  6569BCDE5CBED60E CRC64;
     MDFEQLKQDV IAYSKTIGID KIGFASASPF EELKQRLIQQ QQLNYQSGFE EPDIEKRTNP
     QLLLSGAKSI IAIALAYPSK LKNAPLSKRG ERRGIFCRAS WGQDYHLVLR DRLQKLEAYL
     IEKLPDIEVK SMVDTGELSD RAVSERAGIG WSGKNCSIIT PEFGSYVYLG EMITNVPFPP
     DQPIEDQCGS CTKCIDICPT GALIQGGQLD SKKCIAFLTQ TKGFLPEEYR DKIGNRIYGC
     DTCQTVCPKN KGMDFHNHPE MEPDPELVKP LLTPLLTISN RDFKEKYGIM SGSWRGKKPL
     QRNAILALAH FKEASAIPDL IGVMKDDPRP VLRGTAAWAL GKIGGDGVGE AIEKAMQREK
     DEEVLHEMNR GLELLAQKKE
//
DBGET integrated database retrieval system