ID   QUEF_BORA1              Reviewed;         273 AA.
AC   Q2KXN2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=BAV2453;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50063.1; -; Genomic_DNA.
DR   RefSeq; YP_786965.1; -.
DR   GeneID; 6265985; -.
DR   GenomeReviews; AM167904_GR; BAV2453.
DR   KEGG; bav:BAV2453; -.
DR   NMPDR; fig|521.1.peg.36; -.
DR   HOGENOM; Q2KXN2; -.
DR   OMA; Q2KXN2; EHNEFHE.
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    273       NADPH-dependent 7-cyano-7-deazaguanine
FT                                reductase.
FT                                /FTId=PRO_0000247703.
SQ   SEQUENCE   273 AA;  30350 MW;  6B7132861004BE2D CRC64;
     MPLSDAPLGH NVAYPSEYNA ALLFPIARAE NRAGLGLDGA LPFDGTDIWN AYELSWLDAK
     GKPRIAMASF RIPASSPNII ESKSFKLYLN SFNQTRLPNA QTLRDLLEKD LSAAAGAPVD
     MDFILPQRFD TLRIQELSGI NLDKLDVEVD RYEPAPELLG CTGTGIIEET LMSRLLKSNC
     PVTGQPDWAS VQIAYRGRPI DRAGLLKYII SFRQHAEFHE HCVERIFCDL MQACQPEQLT
     VYARYTRRGG LDINPWRSNA GASAPADLRG ARQ
//