ID   QUEF_BURTA              Reviewed;         274 AA.
AC   Q2T144;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase;
DE            EC=1.7.1.13;
DE   AltName: Full=7-cyano-7-carbaguanine reductase;
DE   AltName: Full=PreQ(0) reductase;
DE   AltName: Full=NADPH-dependent nitrile oxidoreductase;
GN   Name=queF; OrderedLocusNames=BTH_I0548;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-
CC       deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-
CC       cyano-7-carbaguanine + 2 NADPH.
CC   -!- PATHWAY: tRNA modification; queuosine-tRNA biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type
CC       2 subfamily.
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DR   EMBL; CP000086; ABC38829.1; -; Genomic_DNA.
DR   RefSeq; YP_441105.1; -.
DR   GeneID; 3849505; -.
DR   GenomeReviews; CP000086_GR; BTH_I0548.
DR   KEGG; bte:BTH_I0548; -.
DR   TIGR; BTH_I0548; -.
DR   HOGENOM; Q2T144; -.
DR   OMA; Q2T144; EHNEFHE.
DR   BioCyc; BTHA271848:BTH_I0548-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:InterPro.
DR   GO; GO:0046857; F:oxidoreductase activity, acting on other ni...; IEA:HAMAP.
DR   GO; GO:0033739; F:queuine synthase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00817; -; 1.
DR   InterPro; IPR016428; CN_OxRdtase_NADPH-dep_YqcD.
DR   InterPro; IPR001474; GTP_CycHdrlase_I.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   PIRSF; PIRSF004750; Nitrile_oxidored_YqcD_prd; 1.
DR   TIGRFAMs; TIGR03138; QueF; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NADP; Oxidoreductase;
KW   Queuosine biosynthesis.
FT   CHAIN         1    274       NADPH-dependent 7-cyano-7-deazaguanine
FT                                reductase.
FT                                /FTId=PRO_0000247706.
SQ   SEQUENCE   274 AA;  30451 MW;  4D0F932EAF8319E4 CRC64;
     MNPEHSPLGK TTVYANQYDA SLLFPIPRAG AREQIGIGAP LPFFGTDIWN AYELSWLNAR
     GKPQVAIATF YVPAESPNIV ESKSFKLYLG SFAQTAFESI DAVRDALKRD VSAACGASVT
     VRLATPAEFR KLQMDELDGL SLDRLDLDAD VYETDPSFLT ASHDEAPVEE TLVTDLLKSN
     CPVTGQPDWG SVQIHYVGAP IDHAGLLRYI ISFRNHTGFH EQCVERIFID ILRACKPVKL
     AVYARYTRRG GLDINPFRTN YNQPMPDNAR TARQ
//