ID   QUEF_YERPN              Reviewed;         281 AA.
AC   Q1CFD5; C4GWZ4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=YPN_2968;
GN   ORFNames=YP516_3361;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) 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).
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; CP000305; ABG19295.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000017; EEO75444.1; -; Genomic_DNA.
DR   RefSeq; WP_002212122.1; NZ_ACNQ01000017.1.
DR   AlphaFoldDB; Q1CFD5; -.
DR   SMR; Q1CFD5; -.
DR   EnsemblBacteria; ABG19295; ABG19295; YPN_2968.
DR   GeneID; 57977527; -.
DR   KEGG; ypn:YPN_2968; -.
DR   HOGENOM; CLU_054738_0_0_6; -.
DR   OMA; QCVERIY; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000008936; 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..281
FT                   /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT                   /id="PRO_1000062371"
FT   ACT_SITE        189
FT                   /note="Thioimide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   ACT_SITE        196
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         88..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         90..91
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         228..229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   BINDING         257..258
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
SQ   SEQUENCE   281 AA;  32082 MW;  A08B7182F11E5CCA CRC64;
     MSSYQNHKAL AELTLGKPTA YCDYYDATLL QAVPRSMNRE PLGLYPDNLP FHGADIWTLY
     ELSWLNSNGL PQVAVGEISL NADSINLIES KSFKLYLNSF NQTIFADKES VRMTLQRDLA
     ACAQGNVSVA LYDLDEITGQ PISNFNGECL DKQDIRIDSY EFNADYLQGA AGKDHVEESL
     VSHLLKSNCL ITHQPDWGSV QIHYRGPQID HEALLRYLVS FRHHNEFHEQ CVERIFNDIM
     RFCQPETLTV YARYTRRGGL DINPWRSNTD FVPLTGRLAR Q