ID QUEF_BAUCH Reviewed; 283 AA. AC Q1LSV9; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 2. DT 16-JUN-2009, entry version 25. 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=BCI_0525; OS Baumannia cicadellinicola subsp. Homalodisca coagulata. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia. OX NCBI_TaxID=374463; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188; RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., RA Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., RA Moran N.A., Eisen J.A.; RT "Metabolic complementarity and genomics of the dual bacterial RT symbiosis of sharpshooters."; RL PLoS Biol. 4:1079-1092(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. 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; CP000238; ABF13980.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_588955.1; -. DR GeneID; 4056410; -. DR GenomeReviews; CP000238_GR; BCI_0525. DR KEGG; bci:BCI_0525; -. DR HOGENOM; Q1LSV9; -. 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 1 283 NADPH-dependent 7-cyano-7-deazaguanine FT reductase. FT /FTId=PRO_0000247702. SQ SEQUENCE 283 AA; 33067 MW; F23E4B62CCF4A683 CRC64; MTDQQYQLLQ KFKLDKSKIS YRTHYNPMLL QPIPRTIHRE LLGISSISLP FQGADFWTLY ELSWLNKYGL PQVAIGEMII DATSDNLIES QSLKLYLNSI NQTCFSSEQE LRNTLITDIT KCINSQVKIT IHSLSQWMTV PILEFTGECI DNQSIQIDND NYIFNSNLLV NSVEREKVKE TLVSHLLKSN CPITNQPDWG SVQISYYGMR INREALLRYL ISFRKYKIFH EQCVEQIYCD IMQFCLPNTL SVYVRYNRRG GLDINPWRSN ISYSPVNRPL ARQ //