ID   QUEF_CAMJ8              Reviewed;         127 AA.
AC   A8FP38;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   28-JAN-2026, entry version 93.
DE   RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818};
DE            EC=1.7.1.13 {ECO:0000255|HAMAP-Rule:MF_00818};
DE   AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818};
DE   AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00818};
DE   AltName: Full=PreQ(0) reductase {ECO:0000255|HAMAP-Rule:MF_00818};
GN   Name=queF {ECO:0000255|HAMAP-Rule:MF_00818};
GN   OrderedLocusNames=C8J_1628;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 /
OS   NCTC 11828).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=17873037; DOI=10.1128/jb.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA   van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
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_00818}.
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_00818};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00818}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00818}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00818}.
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DR   EMBL; CP000814; ABV53225.1; -; Genomic_DNA.
DR   RefSeq; WP_012006802.1; NC_009839.1.
DR   AlphaFoldDB; A8FP38; -.
DR   SMR; A8FP38; -.
DR   KEGG; cju:C8J_1628; -.
DR   HOGENOM; CLU_102489_1_1_7; -.
DR   UniPathway; UPA00392; -.
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; -; 1.
DR   HAMAP; MF_00818; QueF_type1; 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; IPR016856; QueF_type1.
DR   NCBIfam; TIGR03139; QueF-II; 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   PIRSF; PIRSF027377; Nitrile_oxidored_QueF; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis.
FT   CHAIN           1..127
FT                   /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT                   /id="PRO_1000072870"
FT   ACT_SITE        40
FT                   /note="Thioimide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   ACT_SITE        47
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         62..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         81..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
SQ   SEQUENCE   127 AA;  14986 MW;  81C1F8D5C33B4EBA CRC64;
     MRYGEKEIKE FDVENMEIWP NDAKNDYIIK ITLPEFMCCC PRSGYPDFAT IYLEYMPDKF
     VVELKAIKLY INTFMYRNVS HEASINEIYN TLKDKLKPKW IKVVGDFNPR GNVHTVIECC
     SDMVVPK
//