ID   QUEF_PARP8              Reviewed;         274 AA.
AC   B2JCU2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-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_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=Bphy_0368;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC69561.1; -; Genomic_DNA.
DR   RefSeq; WP_012399787.1; NZ_CADFGH010000001.1.
DR   AlphaFoldDB; B2JCU2; -.
DR   SMR; B2JCU2; -.
DR   STRING; 391038.Bphy_0368; -.
DR   EnsemblBacteria; ACC69561; ACC69561; Bphy_0368.
DR   KEGG; bph:Bphy_0368; -.
DR   eggNOG; COG0780; Bacteria.
DR   eggNOG; COG2904; Bacteria.
DR   HOGENOM; CLU_054738_0_0_4; -.
DR   OMA; QCVERIY; -.
DR   OrthoDB; 1525536at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001192; 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_1000134272"
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;  30589 MW;  6777150E14342030 CRC64;
     MTPEQSPLGK PSSYTEQYDA SLLFPIARKN ARDQIGIGAT LPFFGTDIWN AYELSWLNAR
     GKPQIAIATF YVPADSPNIV ESKSFKLYLG SFAQSSFDSI DVVRDTIKRD VSAACGSSVS
     LHLYPPAEFS KLGLEEFEGT SLDRLDLDAE VYQPDASILK AALDEAPVEE TLFSNLLKSN
     CPVTGQPDWG SVQIHYVGPQ IDHAALLRYI ISYRNHTGFH EQCVEKIFLD VMKVCQPVKL
     AVYARYTRRG GLDINPFRTN FNLPMPDNLR TARQ