ID   QUEF_PSEPK              Reviewed;         276 AA.
AC   Q88KX9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   28-JAN-2026, entry version 124.
DE   RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00817};
DE            EC=1.7.1.13 {ECO:0000255|HAMAP-Rule:MF_00817};
DE   AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00817};
DE   AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00817};
DE   AltName: Full=PreQ(0) reductase {ECO:0000255|HAMAP-Rule:MF_00817};
GN   Name=queF {ECO:0000255|HAMAP-Rule:MF_00817};
GN   OrderedLocusNames=PP_2160;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-
CC       deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
CC       {ECO:0000255|HAMAP-Rule:MF_00817}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-
CC         carbaguanine + 2 NADPH + 3 H(+); Xref=Rhea:RHEA:13409,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:45075, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58703; EC=1.7.1.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00817};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00817}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00817}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00817}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00817}.
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DR   EMBL; AE015451; AAN67773.1; -; Genomic_DNA.
DR   RefSeq; WP_010953147.1; NC_002947.4.
DR   AlphaFoldDB; Q88KX9; -.
DR   SMR; Q88KX9; -.
DR   STRING; 160488.PP_2160; -.
DR   PaxDb; 160488-PP_2160; -.
DR   GeneID; 83681319; -.
DR   KEGG; ppu:PP_2160; -.
DR   PATRIC; fig|160488.4.peg.2277; -.
DR   eggNOG; COG0780; Bacteria.
DR   eggNOG; COG2904; Bacteria.
DR   HOGENOM; CLU_054738_0_0_6; -.
DR   OrthoDB; 9789995at2; -.
DR   PhylomeDB; Q88KX9; -.
DR   BioCyc; PPUT160488:G1G01-2301-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033739; F:preQ1 synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:tRNA queuosine(34) biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1130.10; -; 2.
DR   HAMAP; MF_00817; QueF_type2; 1.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   InterPro; IPR050084; NADPH_dep_7-cyano-7-deazaG_red.
DR   InterPro; IPR029500; QueF.
DR   InterPro; IPR029139; QueF_N.
DR   InterPro; IPR016428; QueF_type2.
DR   NCBIfam; TIGR03138; QueF; 1.
DR   PANTHER; PTHR34354; NADPH-DEPENDENT 7-CYANO-7-DEAZAGUANINE REDUCTASE; 1.
DR   PANTHER; PTHR34354:SF1; NADPH-DEPENDENT 7-CYANO-7-DEAZAGUANINE REDUCTASE; 1.
DR   Pfam; PF14489; QueF; 1.
DR   Pfam; PF14819; QueF_N; 1.
DR   PIRSF; PIRSF004750; Nitrile_oxidored_YqcD_prd; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..276
FT                   /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT                   /id="PRO_0000163046"
FT   ACT_SITE        184
FT                   /note="Thioimide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   ACT_SITE        191
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         83..85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         85..86
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         223..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         252..253
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
SQ   SEQUENCE   276 AA;  30686 MW;  04A44D5229CF0CA7 CRC64;
     MHPAAEHSPL GKSSEYIATY SPEQLFPIPR TAKWAELGVT AQTLPWQGVD YWNCFELSWL
     LPSGKPVVAI GEFAIPADSP NIIESKSFKL YLNSLNQTVF TSLGALQVCL EKDLSAAAGK
     PVGVKVRTLA EVEAQGVVAL PGQCIDALDV AISNYEQPQP ELLRCNPERV VEETLHSHLL
     KSNCPVTGQP DWGSVVVQYK GRALDHASLL TYLISFRQHA DFHEQCVERI YLDLKNLLQP
     EHLTVYARYV RRGGLDINPY RSTGPISPDN KRLVRQ
//