QUEF_CITK8
ID QUEF_CITK8 Reviewed; 282 AA.
AC A8AP02;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=CKO_04150;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) 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_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; CP000822; ABV15215.1; -; Genomic_DNA.
DR RefSeq; WP_012134904.1; NC_009792.1.
DR AlphaFoldDB; A8AP02; -.
DR SMR; A8AP02; -.
DR STRING; 290338.CKO_04150; -.
DR EnsemblBacteria; ABV15215; ABV15215; CKO_04150.
DR GeneID; 45137781; -.
DR KEGG; cko:CKO_04150; -.
DR HOGENOM; CLU_054738_0_0_6; -.
DR OMA; QCVERIY; -.
DR OrthoDB; 1525536at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000008148; 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; -; 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..282
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_1000062337"
FT ACT_SITE 190
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 90..91
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 229..230
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 258..259
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
SQ SEQUENCE 282 AA; 32479 MW; 932DDCF2BC723515 CRC64;
MSSYENHQAL DGLTLGKSTD YRDNYDASLL QGVPRSLNRD PLDLKADNLP FHGADIWTLY
ELSWLNAKGV PQVAVGHVEL DYTSVNLIES KSFKLYLNSF NQTRFDSWDA VRQTLENDLR
ACAQGEVSVA LYRLDELEGQ PAAHFHGTCI DDQDITIDNY QFSTDYLENA ASGEKVVEET
LVSHLLKSNC LITHQPDWGS IQICYRGRKI DREKLLRYLV SFRHHNEFHE QCVERIFNDL
LRFCQPEKLS VYARYTRRGG LDINPWRSNT DFVPATGRLV RQ