ID   QUEF_BUCAP              Reviewed;         262 AA.
AC   Q8K9N6; O69229;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 120.
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}; OrderedLocusNames=BUsg_288;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-262.
RX   PubMed=7765846; DOI=10.1007/bf00296197;
RA   Kolibachuk D., Baumann P.;
RT   "Buchnera aphidicola (aphid-endosymbiont) glyceraldehyde-3-phosphate
RT   dehydrogenase: molecular cloning and sequence analysis.";
RL   Curr. Microbiol. 30:133-136(1995).
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         deazaguanine + 3 H(+) + 2 NADPH; 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; AE013218; AAM67844.1; -; Genomic_DNA.
DR   EMBL; U11045; AAC05800.1; -; Genomic_DNA.
DR   RefSeq; WP_011053811.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9N6; -.
DR   SMR; Q8K9N6; -.
DR   STRING; 198804.BUsg_288; -.
DR   EnsemblBacteria; AAM67844; AAM67844; BUsg_288.
DR   KEGG; bas:BUsg_288; -.
DR   eggNOG; COG0780; Bacteria.
DR   eggNOG; COG2904; Bacteria.
DR   HOGENOM; CLU_054738_0_0_6; -.
DR   OMA; QCVERIY; -.
DR   OrthoDB; 1525536at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046857; F:oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0033739; F:preQ1 synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:queuosine 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; IPR029500; QueF.
DR   InterPro; IPR029139; QueF_N.
DR   InterPro; IPR016428; QueF_type2.
DR   Pfam; PF14489; QueF; 1.
DR   Pfam; PF14819; QueF_N; 1.
DR   PIRSF; PIRSF004750; Nitrile_oxidored_YqcD_prd; 1.
DR   TIGRFAMs; TIGR03138; QueF; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis.
FT   CHAIN           1..262
FT                   /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT                   /id="PRO_0000163023"
FT   ACT_SITE        170
FT                   /note="Thioimide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   ACT_SITE        177
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         69..71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         71..72
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         209..210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         238..239
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   CONFLICT        28
FT                   /note="L -> I (in Ref. 2; AAC05800)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   262 AA;  30731 MW;  2A78FCFA2D946DCE CRC64;
     MSLKINNFNF LRPISRKKHR KKIKLNCLNL PFKGKDIWTL YELSWLNKNG LPQIAIAKIE
     IDVNSANIIE SKSFKIYINS FNQMKFNNNI DFINILTNDL TKCICGQISI KLFSLDAIKN
     ETITDFHGIC IDNQNIKIES YKYTPSFLMI NSERKIIKED LYTHLFKSNC PVTQQPDWAS
     IYIAYTGLSI NHASLLRYLI SFRSHNEFHE ECIERIFNDI NNICKPEELS VYARYTRRGG
     IDINPWRSNT NFSPFLTRLA RQ