QUEF_SALTY
ID QUEF_SALTY Reviewed; 282 AA.
AC Q8ZMD3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=STM2968;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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_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; AE006468; AAL21847.1; -; Genomic_DNA.
DR RefSeq; NP_461888.1; NC_003197.2.
DR RefSeq; WP_000100474.1; NC_003197.2.
DR AlphaFoldDB; Q8ZMD3; -.
DR SMR; Q8ZMD3; -.
DR STRING; 99287.STM2968; -.
DR PaxDb; Q8ZMD3; -.
DR EnsemblBacteria; AAL21847; AAL21847; STM2968.
DR GeneID; 1254491; -.
DR KEGG; stm:STM2968; -.
DR PATRIC; fig|99287.12.peg.3140; -.
DR HOGENOM; CLU_054738_0_0_6; -.
DR OMA; QCVERIY; -.
DR PhylomeDB; Q8ZMD3; -.
DR BioCyc; SENT99287:STM2968-MON; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001014; 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;
KW Reference proteome.
FT CHAIN 1..282
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_0000163059"
FT ACT_SITE 190
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 90..91
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 229..230
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 258..259
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
SQ SEQUENCE 282 AA; 32673 MW; 47A275AB07914C4F CRC64;
MSSYENHQAL DGLTLGKSTD YRDNYDVSLL QGVPRSLNRD PLGLTADNLP FHGADIWTLY
ELSWLNSQGL PQVAVGHVEL DYTSVNLIES KSFKLYLNSF NQTRFDTWET VRQTLERDLR
ACAQGNVSVR LHRLDELEGQ PVAHFHGTCI DDQDISIDNY QFTTDYLQHA VSGEKQVEET
LVSHLLKSNC LITHQPDWGS IQIQYRGRKI DREKLLRYLV SFRHHNEFHE QCVERIFNDI
LRFCQPETLS VYARYTRRGG LDINPWRSNT DFVPATGRLA RQ
