QUEF_PARXL
ID QUEF_PARXL Reviewed; 274 AA.
AC Q145P6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Bxeno_A0405;
GN ORFNames=Bxe_A4056;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE28943.1; -; Genomic_DNA.
DR RefSeq; WP_011486769.1; NZ_CP008760.1.
DR AlphaFoldDB; Q145P6; -.
DR SMR; Q145P6; -.
DR STRING; 266265.Bxe_A4056; -.
DR EnsemblBacteria; ABE28943; ABE28943; Bxe_A4056.
DR KEGG; bxb:DR64_1733; -.
DR KEGG; bxe:Bxe_A4056; -.
DR PATRIC; fig|266265.5.peg.428; -.
DR eggNOG; COG0780; Bacteria.
DR eggNOG; COG2904; Bacteria.
DR OMA; QCVERIY; -.
DR OrthoDB; 1525536at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001817; Chromosome 1.
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..274
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_1000062336"
FT ACT_SITE 181
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 80..82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 82..83
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 220..221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 249..250
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
SQ SEQUENCE 274 AA; 30659 MW; FE8CBC39B6F1EED3 CRC64;
MTPEQSPLGK ASTYTEQYDA SLLFPIARKN AREAIGIGAQ LPFFGTDIWN AYELSWLNAR
GKPQIAVATF FVPADSPNIV ESKSFKLYLG SFAQTAFESM DAVRDTIRRD VSASCGATVS
VHLTAPYKFG KLQMEEFEGL SLDRLDLDTD VYQPDASLLK AALHEAPVEE TVFSNLLKSN
CPVTGQPDWG SVQIHYVGPQ IDHAGLLRYI ISYRNHTGFH EQCVERIFVD VLKACKPVKL
AVYARYTRRG GLDINPFRTN YNLPMPDNMR LARQ