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Database: UniProt
Entry: Q81I72
LinkDB: Q81I72
Original site: Q81I72 
ID   QUEG_BACCR              Reviewed;         380 AA.
AC   Q81I72;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   10-APR-2019, entry version 111.
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=BC_0544;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 /
OS   NCIMB 9373 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL
RC   B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(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; AE016877; AAP07564.1; -; Genomic_DNA.
DR   RefSeq; NP_830363.1; NC_004722.1.
DR   RefSeq; WP_000345215.1; NC_004722.1.
DR   ProteinModelPortal; Q81I72; -.
DR   SMR; Q81I72; -.
DR   PRIDE; Q81I72; -.
DR   EnsemblBacteria; AAP07564; AAP07564; BC_0544.
DR   GeneID; 1202897; -.
DR   KEGG; bce:BC0544; -.
DR   PATRIC; fig|226900.8.peg.500; -.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   KO; K18979; -.
DR   OMA; ICDTDLS; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001417; 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; 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_0000416065.
FT   DOMAIN      178    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;  42398 MW;  551F430DDE70E409 CRC64;
     MDFEQLKQDV IAYSKTIGID KIGFASASPF EELKQRLIQQ QQLNYQSGFE EPDIEKRTNP
     QLLLPGAKSI IAIALAYPSK LKNAPLSKRG ERRGIFCRAS WGQDYHLVLR DRLQKLEAYL
     IEKLPDIEVK SMVDTGELSD RAVSERAGIG WSGKNCSIIT PEFGSYVYLG EMITNVPFPP
     DKPIEDQCGG CTKCIDICPT GALIQGGQLD SKKCIAFLTQ TKGFLPEEYR DKIGNRIYGC
     DTCQTVCPKN KGMDFHNHPE MEPDPELVKP LLTPLLTISN RDFKEKYGIM SGSWRGKKPL
     QRNAILALAH FKEASAIPDL IGVMKDDPRP VLRGTAAWAL GKIGGDGVGE AIEKAMEREK
     DEEVLHEMNR GLELLAQKKE
//
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