ID QUEF_ECOLC Reviewed; 282 AA. AC B1IU47; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 16-JUN-2009, entry version 9. 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=EcolC_0918; OS Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=481805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.; RT "Complete sequence of Escherichia coli C str. ATCC 8739."; RL Submitted (FEB-2008) 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 (By similarity). CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type CC 2 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000946; ACA76587.1; -; Genomic_DNA. DR RefSeq; YP_001723914.1; -. DR GeneID; 6068608; -. DR GenomeReviews; CP000946_GR; EcolC_0918. DR KEGG; ecl:EcolC_0918; -. DR OMA; B1IU47; 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_1000083826. SQ SEQUENCE 282 AA; 32588 MW; 3C2409BCCC13C12D CRC64; MSSYANHQAL AGLTLGKSTD YRDTYDASLL QGVPRSLNRD PLGLKADNLP FHGTDIWTLY ELSWLNAKGL PQVAVGHVEL DYTSVNLIES KSFKLYLNSF NQTRFNNWDE VRQTLERDLS TCAQGKISVA LYRLDELEGQ PIGHFNGTCI DDQDITIDNY EFTTDYLENA TCGEKVVEET LVSHLLKSNC LITHQPDWGS IQIQYRGRQI DREKLLRYLV SFRHHNEFHE QCVERIFNDL LRFCQPEKLS VYARYTRRGG LDINPWRSNS DFVPSTTRLV RQ //