(data stored in ACNUC7421 zone)

SWISSPROT: QUEF_LEGPC

ID   QUEF_LEGPC              Reviewed;         285 AA.
AC   A5IGU1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 76.
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=LPC_2678;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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_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}.
DR   EMBL; CP000675; ABQ56591.1; -; Genomic_DNA.
DR   RefSeq; WP_011945780.1; NC_009494.2.
DR   SMR; A5IGU1; -.
DR   EnsemblBacteria; ABQ56591; ABQ56591; LPC_2678.
DR   KEGG; lpc:LPC_2678; -.
DR   HOGENOM; HOG000273755; -.
DR   KO; K06879; -.
DR   OMA; QCVERIY; -.
DR   BioCyc; LPNE400673:LPC_RS03545-MONOMER; -.
DR   UniPathway; UPA00392; -.
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; A5IGU1.
DR   SWISS-2DPAGE; A5IGU1.
KW   Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis.
FT   CHAIN           1..285
FT                   /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT                   /id="PRO_1000062347"
FT   NP_BIND         93..94
FT                   /note="NADPH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   NP_BIND         259..260
FT                   /note="NADPH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   REGION          91..93
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT   REGION          230..231
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
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"
SQ   SEQUENCE   285 AA;  32712 MW;  ED596B6219951435 CRC64;
     MNKELESIYQ NIANQSELGQ TANYDSYYNP KRLYPIPRAP KRQEINLDPN STTFYGFDCW
     NHYEVSWLNS KGKPVVAMAV ISYDCHSPCI IESKSLKLYF NSLNNSTFPD VETVVQTISK
     DLSYCIGSEV AVNVYPLSDI PNQTIYAAFD GVCLDKLDIE CSVYHVMPDF LSTSSELVEE
     VLYSDLLKSN CLVTNQPDWG SVQIIYKGKK INHEGLLKYL ISFRNHNEFH EQCIERIFAD
     IMRFCQPESL TVYGRYTRRG GLDINPIRST EPCAFDGQNI RLIRQ
//

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