QUEF_BACSU
ID QUEF_BACSU Reviewed; 165 AA.
AC O31678;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase;
DE EC=1.7.1.13;
DE AltName: Full=7-cyano-7-carbaguanine reductase;
DE AltName: Full=NADPH-dependent nitrile oxidoreductase;
DE AltName: Full=PreQ(0) reductase;
GN Name=queF; Synonyms=ykvM; OrderedLocusNames=BSU13750;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP INVOLVEMENT IN QUEUOSINE BIOSYNTHESIS, AND GENE NAME.
RX PubMed=14660578; DOI=10.1074/jbc.m310858200;
RA Reader J.S., Metzgar D., Schimmel P., de Crecy-Lagard V.;
RT "Identification of four genes necessary for biosynthesis of the modified
RT nucleoside queuosine.";
RL J. Biol. Chem. 279:6280-6285(2004).
RN [3]
RP FUNCTION.
RX PubMed=15767583; DOI=10.1073/pnas.0408056102;
RA Van Lanen S.G., Reader J.S., Swairjo M.A., de Crecy-Lagard V., Lee B.,
RA Iwata-Reuyl D.;
RT "From cyclohydrolase to oxidoreductase: discovery of nitrile reductase
RT activity in a common fold.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4264-4269(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, NO METAL
RP COFACTOR, ACTIVITY REGULATION, REACTION MECHANISM, ACTIVE SITE, AND
RP MUTAGENESIS OF CYS-56.
RX PubMed=17929836; DOI=10.1021/bi701265r;
RA Lee B.W., Van Lanen S.G., Iwata-Reuyl D.;
RT "Mechanistic studies of Bacillus subtilis QueF, the nitrile oxidoreductase
RT involved in queuosine biosynthesis.";
RL Biochemistry 46:12844-12854(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH
RP SUBSTRATE TRAPPED AS A COVALENT THIOIMIDE INTERMEDIATE AND MUTANT ALA-56 IN
RP COMPLEX WITH SUBSTRATE BOUND NON-COVALENTLY, REACTION MECHANISM, AND ACTIVE
RP SITES.
RX PubMed=22787148; DOI=10.1074/jbc.m112.388538;
RA Chikwana V.M., Stec B., Lee B.W., de Crecy-Lagard V., Iwata-Reuyl D.,
RA Swairjo M.A.;
RT "Structural basis of biological nitrile reduction.";
RL J. Biol. Chem. 287:30560-30570(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. {ECO:0000269|PubMed:15767583,
CC ECO:0000269|PubMed:17929836}.
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:0000269|PubMed:17929836};
CC -!- COFACTOR:
CC Note=Does not require a metal cofactor.;
CC -!- ACTIVITY REGULATION: Activity is strongly inhibited by Cu(2+) and
CC Fe(3+). {ECO:0000269|PubMed:17929836}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.237 uM for 7-cyano-7-deazaguanine (at pH 7.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:17929836};
CC KM=19.2 uM for NADPH (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17929836};
CC Note=kcat is 0.66 min(-1) (at pH 7.5 and 30 degrees Celsius).;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17929836};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC -!- SUBUNIT: Forms an asymmetric tunnel-fold homodecamer of two head-to-
CC head facing pentamers, harboring 10 active sites at the intersubunit
CC interfaces. {ECO:0000269|PubMed:22787148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 1
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Crystallographic structure revealed that QueF enzyme forms an
CC asymmetric tunnel-fold homodecamer (PubMed:22787148) and not a
CC homododecamer as originally proposed (PubMed:15767583).
CC {ECO:0000305|PubMed:15767583, ECO:0000305|PubMed:22787148}.
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DR EMBL; AL009126; CAB13248.1; -; Genomic_DNA.
DR PIR; D69868; D69868.
DR RefSeq; NP_389258.1; NC_000964.3.
DR RefSeq; WP_003218613.1; NZ_JNCM01000035.1.
DR PDB; 4F8B; X-ray; 2.50 A; A/B/C/D/E=1-165.
DR PDB; 4FGC; X-ray; 2.50 A; A/B/C/D/E=1-165.
DR PDB; 5UDG; X-ray; 2.50 A; A/B/C/D/E=21-165.
DR PDBsum; 4F8B; -.
DR PDBsum; 4FGC; -.
DR PDBsum; 5UDG; -.
DR AlphaFoldDB; O31678; -.
DR SMR; O31678; -.
DR STRING; 224308.BSU13750; -.
DR jPOST; O31678; -.
DR PaxDb; O31678; -.
DR PRIDE; O31678; -.
DR EnsemblBacteria; CAB13248; CAB13248; BSU_13750.
DR GeneID; 50133776; -.
DR GeneID; 64303265; -.
DR GeneID; 939296; -.
DR KEGG; bsu:BSU13750; -.
DR PATRIC; fig|224308.179.peg.1492; -.
DR eggNOG; COG0780; Bacteria.
DR InParanoid; O31678; -.
DR OMA; LECKEFT; -.
DR PhylomeDB; O31678; -.
DR BioCyc; BSUB:BSU13750-MON; -.
DR BRENDA; 1.7.1.13; 658.
DR SABIO-RK; O31678; -.
DR UniPathway; UPA00392; -.
DR PRO; PR:O31678; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3D-structure; Calcium; Cytoplasm; Magnesium; Metal-binding; NADP;
KW Oxidoreductase; Queuosine biosynthesis; Reference proteome.
FT CHAIN 1..165
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_0000162957"
FT ACT_SITE 56
FT /note="Thioimide intermediate"
FT ACT_SITE 63
FT /note="Proton donor"
FT BINDING 78..80
FT /ligand="substrate"
FT BINDING 97..98
FT /ligand="substrate"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MUTAGEN 56
FT /note="C->A,S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17929836"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5UDG"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:4FGC"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4FGC"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:5UDG"
FT STRAND 44..55
FT /evidence="ECO:0007829|PDB:4FGC"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4FGC"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:4FGC"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:4FGC"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:4FGC"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:4FGC"
FT HELIX 97..112
FT /evidence="ECO:0007829|PDB:4FGC"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:4FGC"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4FGC"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4FGC"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:4FGC"
SQ SEQUENCE 165 AA; 19375 MW; E1CEF14D1EAA007D CRC64;
MTTRKESELE GVTLLGNQGT NYLFEYAPDV LESFPNKHVN RDYFVKFNCP EFTSLCPKTG
QPDFATIYIS YIPDEKMVES KSLKLYLFSF RNHGDFHEDC MNIIMNDLIE LMDPRYIEVW
GKFTPRGGIS IDPYTNYGKP GTKYEKMAEY RMMNHDLYPE TIDNR
