ID QUEF_BURCM Reviewed; 274 AA. AC Q0BBX9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 24. 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=Bamb_2788; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) 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. 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; CP000440; ABI88344.1; -; Genomic_DNA. DR RefSeq; YP_774678.1; -. DR GeneID; 4310362; -. DR GenomeReviews; CP000440_GR; Bamb_2788. DR KEGG; bam:Bamb_2788; -. DR NMPDR; fig|339670.3.peg.374; -. DR OMA; Q0BBX9; 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 1 274 NADPH-dependent 7-cyano-7-deazaguanine FT reductase. FT /FTId=PRO_1000062329. SQ SEQUENCE 274 AA; 30415 MW; CCFDA8677B399E19 CRC64; MNPEHSPLGK ATVYAAQYDA SLLFPIPRAG AREQLGITSA LPFFGTDIWN AYELSWLNAR GKPQVAVATF YVPAESPNIV ESKSFKLYLG SFAQSKFDSL DAVRDTLKRD VSAACGASVS VQLVSPHDFG KLQMEELDGL SLDRLDLDTD VYEPDPSLLS AAQDEAPVEE TLVSDLLRSN CPVTGQPDWG SVQIHYVGPQ IDHAGLLRYI ISFRNHTGFH EQCVERIFLD ILHACKPLKL AVYARYTRRG GLDINPFRTN YNQPMPDNAR TARQ //