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QUEF_STRPN
ID   QUEF_STRPN              Reviewed;         154 AA.
AC   Q97P67;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Putative NADPH-dependent 7-cyano-7-deazaguanine reductase;
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=SP_1777;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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}.
CC   -!- CAUTION: Lacks the conserved cysteine residue that is involved in the
CC       formation of the covalent thioimide linkage with the substrate; it is
CC       replaced by a glycine residue (Gly-45). The enzyme may thus be
CC       inactive. {ECO:0000305}.
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DR   EMBL; AE005672; AAK75850.1; -; Genomic_DNA.
DR   PIR; A95207; A95207.
DR   AlphaFoldDB; Q97P67; -.
DR   SMR; Q97P67; -.
DR   STRING; 170187.SP_1777; -.
DR   EnsemblBacteria; AAK75850; AAK75850; SP_1777.
DR   KEGG; spn:SP_1777; -.
DR   eggNOG; COG0780; Bacteria.
DR   OMA; MKHQSAL; -.
DR   PhylomeDB; Q97P67; -.
DR   BioCyc; SPNE170187:G1FZB-1805-MON; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000585; 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; IPR018317; QueC.
DR   InterPro; IPR029500; QueF.
DR   InterPro; IPR016856; QueF_type1.
DR   Pfam; PF06508; QueC; 1.
DR   Pfam; PF14489; QueF; 1.
DR   TIGRFAMs; TIGR03139; QueF-II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis.
FT   CHAIN           1..154
FT                   /note="Putative NADPH-dependent 7-cyano-7-deazaguanine
FT                   reductase"
FT                   /id="PRO_0000163005"
FT   ACT_SITE        52
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         67..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         86..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
SQ   SEQUENCE   154 AA;  18027 MW;  4182F24EF9FDA7BC CRC64;
     MQHYETVEAV TFAYGQRHHL EIQITREIAK EQGIRHHILD MSLLGQITAQ PDFATIHISY
     IPDKLCVESK SLKLYLFSYR NHGDFHENCI NTIGKDLVNL LDPRYLEVWG KFTPRGGISI
     DPYYNYGKQG TKYEGLAEQR LFQHDLYPEK IDNR
 
 
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