QUEF_PROM9
ID QUEF_PROM9 Reviewed; 136 AA.
AC Q318T1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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};
GN OrderedLocusNames=PMT9312_1554;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) 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_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; CP000111; ABB50614.1; -; Genomic_DNA.
DR RefSeq; WP_011377096.1; NC_007577.1.
DR AlphaFoldDB; Q318T1; -.
DR SMR; Q318T1; -.
DR STRING; 74546.PMT9312_1554; -.
DR EnsemblBacteria; ABB50614; ABB50614; PMT9312_1554.
DR KEGG; pmi:PMT9312_1554; -.
DR eggNOG; COG0780; Bacteria.
DR HOGENOM; CLU_102489_1_1_3; -.
DR OMA; LYINSYR; -.
DR OrthoDB; 1675155at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000002715; 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.
FT CHAIN 1..136
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_0000247688"
FT ACT_SITE 50
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT ACT_SITE 57
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 72..74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
SQ SEQUENCE 136 AA; 15855 MW; 0B656203F7818671 CRC64;
MSTAKLDDST QRPLYGERII EESKIICFEN PNKKRIYEIS IQLPEFTCKC PFSGYPDFAK
LNIIYQPNLS VYELKSLKLY INNFRDIKIS HEEVVNRIMD DLVNEGSPHW IHLNAAFNPR
GNVSMQLDIF SGQKRN
