ID QUEF_ECOHS Reviewed; 282 AA. AC A8A3S9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 16-JUN-2009, entry version 15. 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=EcHS_A2938; OS Escherichia coli O9:H4 (strain HS). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331112; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18676672; DOI=10.1128/JB.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic RT analysis of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(2008). 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; CP000802; ABV07183.1; -; Genomic_DNA. DR RefSeq; YP_001459566.1; -. DR GeneID; 5593734; -. DR GenomeReviews; CP000802_GR; EcHS_A2938. DR KEGG; ecx:EcHS_A2938; -. DR OMA; A8A3S9; 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_1000062339. 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 //