(data stored in ACNUC7421 zone)

SWISSPROT: 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   08-MAY-2019, entry version 89.
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};
GN   OrderedLocusNames=Bxeno_A0405; 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.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome 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
CC       2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00817}.
DR   EMBL; CP000270; ABE28943.1; -; Genomic_DNA.
DR   RefSeq; WP_011486769.1; NZ_CP008760.1.
DR   SMR; Q145P6; -.
DR   STRING; 266265.Bxe_A4056; -.
DR   EnsemblBacteria; ABE28943; ABE28943; Bxe_A4056.
DR   GeneID; 4002213; -.
DR   KEGG; bxb:DR64_1733; -.
DR   KEGG; bxe:Bxe_A4056; -.
DR   PATRIC; fig|266265.5.peg.428; -.
DR   eggNOG; ENOG4105CSD; Bacteria.
DR   eggNOG; COG0780; LUCA.
DR   eggNOG; COG2904; LUCA.
DR   HOGENOM; HOG000273755; -.
DR   KO; K06879; -.
DR   OMA; QCVERIY; -.
DR   OrthoDB; 1525536at2; -.
DR   BioCyc; BXEN266265:BXE_RS02030-MONOMER; -.
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   HAMAP; MF_00817; QueF_type2; 1.
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;
DR   PRODOM; Q145P6.
DR   SWISS-2DPAGE; Q145P6.
KW   Complete proteome; Cytoplasm; NADP; Oxidoreductase;
KW   Queuosine biosynthesis; Reference proteome.
FT   CHAIN         1    274       NADPH-dependent 7-cyano-7-deazaguanine
FT                                reductase.
FT                                /FTId=PRO_1000062336.
FT   NP_BIND      82     83       NADPH. {ECO:0000255|HAMAP-Rule:MF_00817}.
FT   NP_BIND     249    250       NADPH. {ECO:0000255|HAMAP-Rule:MF_00817}.
FT   REGION       80     82       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00817}.
FT   REGION      220    221       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00817}.
FT   ACT_SITE    181    181       Thioimide intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00817}.
FT   ACT_SITE    188    188       Proton donor. {ECO:0000255|HAMAP-
FT                                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
//

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