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QUEF_RHOBA
ID   QUEF_RHOBA              Reviewed;         121 AA.
AC   Q7UVG9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818};
DE            EC=1.7.1.13 {ECO:0000255|HAMAP-Rule:MF_00818};
DE   AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818};
DE   AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00818};
DE   AltName: Full=PreQ(0) reductase {ECO:0000255|HAMAP-Rule:MF_00818};
GN   Name=queF {ECO:0000255|HAMAP-Rule:MF_00818}; OrderedLocusNames=RB2642;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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_00818}.
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_00818};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00818}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00818}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00818}.
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DR   EMBL; BX294137; CAD72755.1; -; Genomic_DNA.
DR   RefSeq; NP_865071.1; NC_005027.1.
DR   RefSeq; WP_007324336.1; NC_005027.1.
DR   AlphaFoldDB; Q7UVG9; -.
DR   SMR; Q7UVG9; -.
DR   STRING; 243090.RB2642; -.
DR   EnsemblBacteria; CAD72755; CAD72755; RB2642.
DR   KEGG; rba:RB2642; -.
DR   PATRIC; fig|243090.15.peg.1213; -.
DR   eggNOG; COG0780; Bacteria.
DR   HOGENOM; CLU_102489_1_0_0; -.
DR   InParanoid; Q7UVG9; -.
DR   OMA; LECKEFT; -.
DR   OrthoDB; 1675155at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001025; Chromosome.
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; -; 1.
DR   HAMAP; MF_00818; QueF_type1; 1.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   InterPro; IPR029500; QueF.
DR   InterPro; IPR016856; QueF_type1.
DR   Pfam; PF14489; QueF; 1.
DR   PIRSF; PIRSF027377; Nitrile_oxidored_QueF; 1.
DR   TIGRFAMs; TIGR03139; QueF-II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..121
FT                   /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT                   /id="PRO_0000162991"
FT   ACT_SITE        36
FT                   /note="Thioimide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   ACT_SITE        43
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         58..60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT   BINDING         77..78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
SQ   SEQUENCE   121 AA;  13897 MW;  337B6222EC9536CA CRC64;
     MSDTASFRDT LEVFENPAPT RNFTIEHHCP EFTSVCPKTG QPDYGTIVFT YVPDRVCVEL
     KSLKMYLQKF RNEGIFYEQV TNRILDDFVA VVQPRKVTVE SKWTPRGGLN SNIIVTYPDE
     A
 
 
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