QUEF_RHOPT
ID QUEF_RHOPT Reviewed; 158 AA.
AC B3Q6L1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Rpal_3217;
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=395960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001096; ACF01720.1; -; Genomic_DNA.
DR RefSeq; WP_012496319.1; NC_011004.1.
DR AlphaFoldDB; B3Q6L1; -.
DR SMR; B3Q6L1; -.
DR EnsemblBacteria; ACF01720; ACF01720; Rpal_3217.
DR KEGG; rpt:Rpal_3217; -.
DR HOGENOM; CLU_102489_0_1_5; -.
DR OMA; LECKEFT; -.
DR OrthoDB; 1675155at2; -.
DR BioCyc; RPAL395960:RPAL_RS15895-MON; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001725; 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 TIGRFAMs; TIGR03139; QueF-II; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis.
FT CHAIN 1..158
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_1000134311"
FT ACT_SITE 56
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT ACT_SITE 63
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 78..80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
SQ SEQUENCE 158 AA; 17780 MW; D5A4C82F44E610C9 CRC64;
MSKTPRKSAA SPSLQLGQAV EWPDRPEAAK LDRVPNPQKD THFLARFTAP EFTSLCPVTG
QPDFAHLVID YVPGPWLLES KSLKLYLASF RNHGAFHEDC TVAIGKRIAT EIKPKWLRIG
GYWYPRGGIP IDVFWQTGKL PKDVWVPDQG VQPYRGRG
