ID   QUEF_PORGI              Reviewed;         154 AA.
AC   Q7MUX8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=PG_1347;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE015924; AAQ66412.1; -; Genomic_DNA.
DR   RefSeq; WP_005874066.1; NC_002950.2.
DR   AlphaFoldDB; Q7MUX8; -.
DR   SMR; Q7MUX8; -.
DR   STRING; 242619.PG_1347; -.
DR   EnsemblBacteria; AAQ66412; AAQ66412; PG_1347.
DR   GeneID; 29256342; -.
DR   KEGG; pgi:PG_1347; -.
DR   eggNOG; COG0780; Bacteria.
DR   HOGENOM; CLU_102489_0_1_10; -.
DR   OMA; LECKEFT; -.
DR   OrthoDB; 1675155at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000588; 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..154
FT                   /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT                   /id="PRO_0000162985"
FT   ACT_SITE        54
FT                   /note="Thioimide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   ACT_SITE        61
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         76..78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         95..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
SQ   SEQUENCE   154 AA;  17924 MW;  F894834C248A9735 CRC64;
     MTGIREGEKE LSLLGSKTEY RNDYAPEVLE AFTNKHQEND YWVRFNCPEF TSLCPITGQP
     DFATIYINYI PDVKMVESKS LKLYLFSFRN HGAFHEDCVN IIMKDLIALM QPRYIEVWGD
     FTPRGGISIV PFCNYGKPGS RYELLAEKRM ETHH