ID QUEF_ALHEH Reviewed; 129 AA. AC Q0AAV5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. 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=Mlg_0678; OS Alkalilimnicola ehrlichei (strain MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272; 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., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., RA King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., RA Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; 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 1 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; CP000453; ABI56032.1; -; Genomic_DNA. DR RefSeq; YP_741522.1; -. DR GeneID; 4268473; -. DR GenomeReviews; CP000453_GR; Mlg_0678. DR KEGG; aeh:Mlg_0678; -. DR NMPDR; fig|187272.6.peg.649; -. DR HOGENOM; Q0AAV5; -. DR OMA; Q0AAV5; RVGRRYD. 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_00818; -; 1. DR InterPro; IPR016856; CN_OxRdtase_NADPH-dep_QueF. DR InterPro; IPR001474; GTP_CycHdrlase_I. DR Pfam; PF01227; GTP_cyclohydroI; 1. DR PIRSF; PIRSF027377; Nitrile_oxidored_QueF; 1. DR ProDom; PD003330; GTP_cyclohydroI; 1. DR TIGRFAMs; TIGR03139; QueF-II; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Queuosine biosynthesis. FT CHAIN 1 129 NADPH-dependent 7-cyano-7-deazaguanine FT reductase. FT /FTId=PRO_1000062374. SQ SEQUENCE 129 AA; 14915 MW; 9ED07706B4458CB6 CRC64; MSTQPSKDLE TFPNPRPERD FVLHMRIPEF TCLCPKTGQP DFATIHLDYV PDERCVELKS LKLYMWSFRD QGAFHEAITN EILDDLVRAT EPRYMKVTAE FYVRGGIYTT VVAEHRKPGW APAPKVELA //