QUEF_GEOKA
ID QUEF_GEOKA Reviewed; 165 AA.
AC Q5L1B7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Nitrile reductase;
DE Short=NRed;
DE AltName: Full=PreQ(0) reductase {ECO:0000255|HAMAP-Rule:MF_00818};
GN Name=queF {ECO:0000255|HAMAP-Rule:MF_00818}; OrderedLocusNames=GK0978;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND MUTAGENESIS OF CYS-56.
RX DOI=10.1002/adsc.201200109;
RA Wilding B., Winkler M., Petschacher B., Kratzer R., Glieder A.,
RA Klempier N.;
RT "Nitrile reductase from Geobacillus kaustophilus: a potential catalyst for
RT a new nitrile biotransformation reaction.";
RL Adv. Synth. Catal. 354:2191-2198(2012).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-
CC deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1), a late
CC step in the queuosine pathway. Is highly specific for its natural
CC substrate preQ0, since it cannot use various aliphatic, aromatic and
CC heterocyclic nitriles, although it can reduce the substrate analog 5-
CC cyanopyrrolo[2,3-d]pyrimidin-4-one with lesser efficiency.
CC {ECO:0000255|HAMAP-Rule:MF_00818, ECO:0000269|Ref.2}.
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, ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: Is totally inhibited by 4-aminobenzylcyanide in
CC vitro. {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for 7-cyano-7-deazaguanine (at 55 degrees Celsius)
CC {ECO:0000269|Ref.2};
CC KM=34 uM for NADPH (at 55 degrees Celsius) {ECO:0000269|Ref.2};
CC KM=336 uM for 5-cyanopyrrolo[2,3-d]pyrimidin-4-one (at 55 degrees
CC Celsius) {ECO:0000269|Ref.2};
CC Note=kcat is 3.9 min(-1) for the reduction of 7-cyano-7-deazaguanine,
CC and 9.3 min(-1) for that of 5-cyanopyrrolo[2,3-d]pyrimidin-4-one (at
CC 55 degrees Celsius).;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Enzymatic activity increases 12-fold in response to a change in
CC temperature from 25 to 65 degrees Celsius. Displays a half life of 43
CC hours at 55 degrees Celsius. {ECO:0000269|Ref.2};
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; BA000043; BAD75263.1; -; Genomic_DNA.
DR RefSeq; WP_011230479.1; NC_006510.1.
DR AlphaFoldDB; Q5L1B7; -.
DR SMR; Q5L1B7; -.
DR STRING; 235909.GK0978; -.
DR EnsemblBacteria; BAD75263; BAD75263; GK0978.
DR KEGG; gka:GK0978; -.
DR eggNOG; COG0780; Bacteria.
DR HOGENOM; CLU_102489_0_1_9; -.
DR OMA; LECKEFT; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001172; 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 1: Evidence at protein level;
KW Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis;
KW Reference proteome.
FT CHAIN 1..165
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_0000162972"
FT ACT_SITE 56
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT ACT_SITE 63
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 78..80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818"
FT MUTAGEN 56
FT /note="C->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 165 AA; 19414 MW; 4107F82E1112CBE1 CRC64;
MAGRKEEELK DLTLLGNQGT TYSFTYNPNL LEVFDNKHPD RDYFVKFNCP EFTTLCPKTG
QPDFATIYIS YIPDKKCVES KSLKLYLFSF RNHGDFHEDC VNIIMNDLIK VMEPRYIEVW
GKFTPRGGIS IDPYCNWGRP GTKYEKMAEY RLLNHDLYPE KVDNR
