QUEF_LEGPL
ID QUEF_LEGPL Reviewed; 285 AA.
AC Q5WYT2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=lpl0654;
OS Legionella pneumophila (strain Lens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH14888.1; -; Genomic_DNA.
DR RefSeq; WP_011214837.1; NC_006369.1.
DR AlphaFoldDB; Q5WYT2; -.
DR SMR; Q5WYT2; -.
DR EnsemblBacteria; CAH14888; CAH14888; lpl0654.
DR KEGG; lpf:lpl0654; -.
DR LegioList; lpl0654; -.
DR HOGENOM; CLU_054738_0_0_6; -.
DR OMA; EGRQIDR; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000002517; 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..285
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_0000163038"
FT ACT_SITE 191
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 91..93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 93..94
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 230..231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 259..260
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
SQ SEQUENCE 285 AA; 32733 MW; 44DCAE8E606928F3 CRC64;
MNKELEIIYQ NIANQSELGQ SSNYDDHYNP KRLYPIPRAP KRQEINLDPN STTFYGFDCW
NHYEVSWLNS KGKPVVAMAV ISYDCHSPCI IESKSLKLYF NSLNNTTFPD VETVVQTISK
DLSHCIGSEV AVNVYPLSEI ASQTIYAAFD GICLDKLDIE CSVYHVMPDF LSTSSELVEE
VLYSDLLKSN CLVTNQPDWG SVQIIYKGKK INHEGLLKYL ISFRNHNEFH EQCIERIFAD
IMRFCQPESL TVYGRYTRRG GLDINPIRST EPCVFDGQNI RLIRQ