QUEF_NITSB
ID QUEF_NITSB Reviewed; 131 AA.
AC A6Q0W4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=NIS_0005;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF69123.1; -; Genomic_DNA.
DR RefSeq; WP_011979549.1; NC_009662.1.
DR AlphaFoldDB; A6Q0W4; -.
DR SMR; A6Q0W4; -.
DR STRING; 387092.NIS_0005; -.
DR EnsemblBacteria; BAF69123; BAF69123; NIS_0005.
DR KEGG; nis:NIS_0005; -.
DR eggNOG; COG0780; Bacteria.
DR HOGENOM; CLU_102489_1_1_7; -.
DR OMA; LYINSYR; -.
DR OrthoDB; 1675155at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001118; 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..131
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_1000062398"
FT ACT_SITE 41
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT ACT_SITE 48
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 63..65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
SQ SEQUENCE 131 AA; 15595 MW; 7604202906AD5F06 CRC64;
MRYGEKEIQE FDPKKDLEIW PNKHNKPYKI KITLPEFSCL CPRSGYPDYA TMHLEYIPDQ
YVVELKALKL YINSFRNRYI SHEDSTNEIF DTLYSKLKPK YMRLVADFNP RGNVHTLIEI
DSEEIEKVSN G
