ID   QUEF_STRMU              Reviewed;         162 AA.
AC   Q8DUL0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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}; OrderedLocusNames=SMU_915c;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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_00818}.
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_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; AE014133; AAN58623.1; -; Genomic_DNA.
DR   RefSeq; NP_721317.1; NC_004350.2.
DR   RefSeq; WP_002263288.1; NC_004350.2.
DR   AlphaFoldDB; Q8DUL0; -.
DR   SMR; Q8DUL0; -.
DR   STRING; 210007.SMU_915c; -.
DR   PRIDE; Q8DUL0; -.
DR   EnsemblBacteria; AAN58623; AAN58623; SMU_915c.
DR   KEGG; smu:SMU_915c; -.
DR   PATRIC; fig|210007.7.peg.816; -.
DR   eggNOG; COG0780; Bacteria.
DR   HOGENOM; CLU_102489_0_1_9; -.
DR   OMA; LECKEFT; -.
DR   PhylomeDB; Q8DUL0; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000002512; 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; -; 1.
DR   HAMAP; MF_00818; QueF_type1; 1.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   InterPro; IPR029500; QueF.
DR   InterPro; IPR016856; QueF_type1.
DR   Pfam; PF14489; QueF; 1.
DR   PIRSF; PIRSF027377; Nitrile_oxidored_QueF; 1.
DR   TIGRFAMs; TIGR03139; QueF-II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..162
FT                   /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT                   /id="PRO_0000163004"
FT   ACT_SITE        53
FT                   /note="Thioimide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   ACT_SITE        60
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         75..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         94..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
SQ   SEQUENCE   162 AA;  19171 MW;  2E507A0C83D58450 CRC64;
     MSQEEIKDLT LLGNQKTNYN FDYDLNILEA FDNRHQDNDY FIKFNCPEFT SLCPITGQPD
     FATIYLSYIP DKKCVESKSL KLYLFSYRNH GDFHENCINT IGKDLVDLLQ PRYLEVWGKF
     TPRGGISIDP YYNYGRPNTK YEEMAAYRLM NHDLYPETID NR