ID   QUEF_ECOK1              Reviewed;         282 AA.
AC   A1AEY1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Ecok1_27270; ORFNames=APECO1_3737;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ02221.1; -; Genomic_DNA.
DR   RefSeq; YP_854010.1; -.
DR   GeneID; 4494418; -.
DR   GenomeReviews; CP000468_GR; Ecok1_27270.
DR   KEGG; ecv:APECO1_3737; -.
DR   OMA; A1AEY1; 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    282       NADPH-dependent 7-cyano-7-deazaguanine
FT                                reductase.
FT                                /FTId=PRO_1000062340.
SQ   SEQUENCE   282 AA;  32557 MW;  575A0751641EB5C3 CRC64;
     MSSYANHQAL AGLTLGKSTD YRDTYDASLL QGVPRSLNRD PLGLKADNLP FHGTDIWTLY
     ELSWLNAKGL PQVAVGHVEL DYTSVNLIES KSFKLYLNSF NQTRFNNWDE VRQTLERDLS
     TCAQGKVSVA LYRLDELEGQ PIGHFNGTCI DDQDITIDNY EFTTDYLENA TSGEKVVEET
     LVSHLLKSNC LITHQPDWGS IQIQYRGRQI DREKLLRYLV SFRHHNEFHE QCVERIFNDL
     LRFCQPEKLS VYARYTRRGG LDINPWRSNS DFVPSTTRLV RQ
//