ID   QUEF_CHRSD              Reviewed;         277 AA.
AC   Q1QXV0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=Csal_1353;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-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.
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DR   EMBL; CP000285; ABE58708.1; -; Genomic_DNA.
DR   RefSeq; YP_573407.1; -.
DR   GeneID; 4029142; -.
DR   GenomeReviews; CP000285_GR; Csal_1353.
DR   KEGG; csa:Csal_1353; -.
DR   NMPDR; fig|290398.4.peg.1343; -.
DR   HOGENOM; Q1QXV0; -.
DR   OMA; Q1QXV0; EHNEFHE.
DR   BioCyc; CSAL290398:CSAL_1353-MON; -.
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    277       NADPH-dependent 7-cyano-7-deazaguanine
FT                                reductase.
FT                                /FTId=PRO_0000247707.
SQ   SEQUENCE   277 AA;  31386 MW;  E174E4900D12E324 CRC64;
     MSERDKTLEH APLGRESAYP EHYDAGLLFP IPRQANRAPL GLDDAALPFE GEDEWHAFEL
     SWLDAKGKPI VAVARFRLPA DSPSLIESKS WKLYLNSFNQ TRFDRREAVI DTLERDLAQA
     AGASVAVALF GVEDDALMPR ALPGECLDDL DVSIEYYTPT PGLLEVGEEI VEETLHSHLL
     KSNCPVTGQP DWGSVLIRYR GPRLERDALL KYLISYRQHQ DFHEHCVEHL FVDLMARARP
     ERLLVMARYV RRGGLDISPW RGTPGERPPT PLRLARQ
//