QUEF_VIBCH
ID QUEF_VIBCH Reviewed; 281 AA.
AC Q9KTK0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 121.
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=VC_0902;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) IN COMPLEX WITH GUANINE, FUNCTION,
RP SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=20875425; DOI=10.1016/j.jmb.2010.09.042;
RA Kim Y., Zhou M., Moy S., Morales J., Cunningham M.A., Joachimiak A.;
RT "High-resolution structure of the nitrile reductase QueF combined with
RT molecular simulations provide insight into enzyme mechanism.";
RL J. Mol. Biol. 404:127-137(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-188;
RP ALA-227 AND LEU-256 IN COMPLEXES WITH NADP AND SUBSTRATE PREQ0 TRAPPED AS A
RP COVALENT THIOIMIDE INTERMEDIATE, AND ACTIVE SITE CYS-188.
RG Center for structural genomics of infectious diseases (CSGID);
RT "Crystal structures of 7-cyano-7-deazaguanine reductase, QueF, from Vibrio
RT cholerae.";
RL Submitted (JAN-2013) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-
CC deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
CC {ECO:0000305|PubMed:20875425}.
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 ECO:0000269|PubMed:20875425}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF94064.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF94064.1; ALT_INIT; Genomic_DNA.
DR PIR; F82265; F82265.
DR RefSeq; NP_230549.2; NC_002505.1.
DR RefSeq; WP_000049898.1; NZ_LT906614.1.
DR PDB; 3BP1; X-ray; 1.53 A; A/B/C/D=1-281.
DR PDB; 3RJ4; X-ray; 1.75 A; A/B=1-281.
DR PDB; 3RZP; X-ray; 2.00 A; A/B/C/D=1-281.
DR PDB; 3S19; X-ray; 1.50 A; A/B/C/D=1-281.
DR PDB; 3UXJ; X-ray; 1.40 A; A/B/C/D=1-281.
DR PDB; 3UXV; X-ray; 1.56 A; A/B/C/D=1-281.
DR PDB; 4GHM; X-ray; 1.62 A; A/B=1-281.
DR PDB; 4IQI; X-ray; 1.50 A; A/B=1-281.
DR PDBsum; 3BP1; -.
DR PDBsum; 3RJ4; -.
DR PDBsum; 3RZP; -.
DR PDBsum; 3S19; -.
DR PDBsum; 3UXJ; -.
DR PDBsum; 3UXV; -.
DR PDBsum; 4GHM; -.
DR PDBsum; 4IQI; -.
DR AlphaFoldDB; Q9KTK0; -.
DR SMR; Q9KTK0; -.
DR STRING; 243277.VC_0902; -.
DR DNASU; 2614193; -.
DR EnsemblBacteria; AAF94064; AAF94064; VC_0902.
DR GeneID; 57739594; -.
DR KEGG; vch:VC_0902; -.
DR PATRIC; fig|243277.26.peg.859; -.
DR eggNOG; COG0780; Bacteria.
DR eggNOG; COG2904; Bacteria.
DR HOGENOM; CLU_054738_0_0_6; -.
DR OMA; QCVERIY; -.
DR BRENDA; 1.7.1.13; 6626.
DR UniPathway; UPA00392; -.
DR EvolutionaryTrace; Q9KTK0; -.
DR Proteomes; UP000000584; Chromosome 1.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis;
KW Reference proteome.
FT CHAIN 1..281
FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase"
FT /id="PRO_0000163062"
FT REGION 262..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817,
FT ECO:0000269|Ref.3"
FT ACT_SITE 195
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00817"
FT BINDING 87..89
FT /ligand="substrate"
FT BINDING 89..90
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT BINDING 227..228
FT /ligand="substrate"
FT BINDING 256..257
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3UXJ"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3S19"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3UXJ"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:3UXJ"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:3UXJ"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3UXJ"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3UXJ"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 170..188
FT /evidence="ECO:0007829|PDB:3UXJ"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 194..208
FT /evidence="ECO:0007829|PDB:3UXJ"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:3UXJ"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4IQI"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:3UXJ"
FT STRAND 259..268
FT /evidence="ECO:0007829|PDB:3UXJ"
SQ SEQUENCE 281 AA; 31969 MW; 9059809F7D2D5B02 CRC64;
MSKYSDAKEL ASLTLGKKTE YANQYDPSLL QPVPRSLNRN DLHLSATLPF QGCDIWTLYE
LSWLNQKGLP QVAIGEVSIP ATSANLIESK SFKLYLNSYN QTRFASWDEV QTRLVHDLSA
CAGETVTVNV KSLNEYTAEP IVTMQGECID DQDIEIANYE FDDALLQGAA QGEEVSEVLH
SHLLKSNCLI TNQPDWGSVE IAYHGAKMNR EALLRYLVSF REHNEFHEQC VERIFTDIMR
YCQPQSLTVY ARYTRRGGLD INPFRSSHQS APNHNQRMAR Q
