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Database: UniProt
Entry: B1XQP9_SYNP2
LinkDB: B1XQP9_SYNP2
Original site: B1XQP9_SYNP2 
ID   B1XQP9_SYNP2            Unreviewed;       314 AA.
AC   B1XQP9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   10-OCT-2018, entry version 71.
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=SYNPCC7002_A1957 {ECO:0000313|EMBL:ACA99944.1};
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=32049 {ECO:0000313|EMBL:ACA99944.1, ECO:0000313|Proteomes:UP000001688};
RN   [1] {ECO:0000313|Proteomes:UP000001688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6
RC   {ECO:0000313|Proteomes:UP000001688};
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C.,
RA   Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) 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; CP000951; ACA99944.1; -; Genomic_DNA.
DR   RefSeq; WP_012307567.1; NC_010475.1.
DR   ProteinModelPortal; B1XQP9; -.
DR   STRING; 32049.SYNPCC7002_A1957; -.
DR   EnsemblBacteria; ACA99944; ACA99944; SYNPCC7002_A1957.
DR   KEGG; syp:SYNPCC7002_A1957; -.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   HOGENOM; HOG000272644; -.
DR   KO; K18979; -.
DR   OMA; VDGSKCI; -.
DR   OrthoDB; POG091H01VA; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001688; 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   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 {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001688};
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:UP000001688};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   DOMAIN      175    207       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL       187    187       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       190    190       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       193    193       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       197    197       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       241    241       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       244    244       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       248    248       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   314 AA;  35542 MW;  5EAA49829C167626 CRC64;
     MSQLQTDRTI RVKNYALSLG FHLVGIADAT VDNAHNQQQL QAWLAAGYQA EMAWMANPKR
     QDIQACLPGV QSVICVALNY YTPHAHSEAP GVGKISRYGW GRDYHRVLGK RLKAFCQWLT
     KEFPEEHHRF YVDTGPVQDK VWAERAGLGW IAKNSNVITR EYGSWVFLGE VLTTLALTPD
     QPHTKHCGTC TRCIEACPTE AIAAPFTVDA NRCIAYHTIE NRAEQLPPHI APHLQNWVAG
     CDICQDVCPW NQRFAQPTNI EDFQPYPKHL APKLAELATL SETEWDQRLT GSALRRIKPA
     MWRRNAQANL DHQP
//
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