ID   B4RF68_PHEZH            Unreviewed;       151 AA.
AC   B4RF68;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 97.
DE   RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000256|HAMAP-Rule:MF_00818};
DE            EC=1.7.1.13 {ECO:0000256|HAMAP-Rule:MF_00818};
DE   AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000256|HAMAP-Rule:MF_00818};
DE   AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00818};
DE   AltName: Full=PreQ(0) reductase {ECO:0000256|HAMAP-Rule:MF_00818};
GN   Name=queF {ECO:0000256|HAMAP-Rule:MF_00818};
GN   OrderedLocusNames=PHZ_c2228 {ECO:0000313|EMBL:ACG78638.1};
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Caulobacterales; Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG78638.1, ECO:0000313|Proteomes:UP000001868};
RN   [1] {ECO:0000313|EMBL:ACG78638.1, ECO:0000313|Proteomes:UP000001868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1 {ECO:0000313|EMBL:ACG78638.1,
RC   ECO:0000313|Proteomes:UP000001868};
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-
CC       deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
CC       {ECO:0000256|HAMAP-Rule:MF_00818}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-
CC         carbaguanine + 2 NADPH + 3 H(+); 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:0000256|HAMAP-Rule:MF_00818};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00818}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00818}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00818}.
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DR   EMBL; CP000747; ACG78638.1; -; Genomic_DNA.
DR   RefSeq; WP_012522779.1; NC_011144.1.
DR   AlphaFoldDB; B4RF68; -.
DR   STRING; 450851.PHZ_c2228; -.
DR   KEGG; pzu:PHZ_c2228; -.
DR   eggNOG; COG0780; Bacteria.
DR   HOGENOM; CLU_102489_0_1_5; -.
DR   OrthoDB; 9789995at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001868; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033739; F:preQ1 synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:tRNA queuosine(34) 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; IPR050084; NADPH_dep_7-cyano-7-deazaG_red.
DR   InterPro; IPR029500; QueF.
DR   InterPro; IPR016856; QueF_type1.
DR   NCBIfam; TIGR03139; QueF-II; 1.
DR   PANTHER; PTHR34354; NADPH-DEPENDENT 7-CYANO-7-DEAZAGUANINE REDUCTASE; 1.
DR   PANTHER; PTHR34354:SF1; NADPH-DEPENDENT 7-CYANO-7-DEAZAGUANINE REDUCTASE; 1.
DR   Pfam; PF14489; QueF; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00818};
KW   Hydrolase {ECO:0000313|EMBL:ACG78638.1};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00818};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00818};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00818}; Reference proteome {ECO:0000313|Proteomes:UP000001868}.
FT   DOMAIN          55..131
FT                   /note="NADPH-dependent 7-cyano-7-deazaguanine reductase
FT                   QueF"
FT                   /evidence="ECO:0000259|Pfam:PF14489"
FT   ACT_SITE        49
FT                   /note="Thioimide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00818"
FT   ACT_SITE        56
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00818"
FT   BINDING         71..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00818"
FT   BINDING         90..91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00818"
SQ   SEQUENCE   151 AA;  16874 MW;  DEC0551711721D23 CRC64;
     MEETHLSQLG RDVRGFDSPE AAVVERVPNP HKGETYLVRF TAPEFTSLCP VTGQPDFAHL
     VIDYVPGEWL VESKSLKLYL ASFRNHGAFH EDCTVAIGKR LVAELAPQWL RIGGYWYPRG
     GIPIDVFWQT GPAPEGLWLP DQGVAPYRGR G
//