QUEG_THEVB
ID QUEG_THEVB Reviewed; 312 AA.
AC Q8DLA9;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Epoxyqueuosine reductase {ECO:0000255|HAMAP-Rule:MF_00916};
DE EC=1.17.99.6 {ECO:0000255|HAMAP-Rule:MF_00916};
DE AltName: Full=Queuosine biosynthesis protein QueG {ECO:0000255|HAMAP-Rule:MF_00916};
GN Name=queG {ECO:0000255|HAMAP-Rule:MF_00916}; OrderedLocusNames=tlr0587;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
CC -!- FUNCTION: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine
CC (Q), which is a hypermodified base found in the wobble positions of
CC tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr). {ECO:0000255|HAMAP-
CC Rule:MF_00916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in
CC tRNA; Xref=Rhea:RHEA:32159, Rhea:RHEA-COMP:10345, Rhea:RHEA-
CC COMP:10346, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:82831, ChEBI:CHEBI:82834; EC=1.17.99.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00916};
CC -!- COFACTOR:
CC Name=cob(II)alamin; Xref=ChEBI:CHEBI:16304;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00916};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00916};
CC Note=Binds 2 [4Fe-4S] clusters per monomer. {ECO:0000255|HAMAP-
CC Rule:MF_00916};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00916}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00916}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00916}.
CC -!- SIMILARITY: Belongs to the QueG family. {ECO:0000255|HAMAP-
CC Rule:MF_00916}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC08139.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000039; BAC08139.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_681377.1; NC_004113.1.
DR AlphaFoldDB; Q8DLA9; -.
DR SMR; Q8DLA9; -.
DR STRING; 197221.22294308; -.
DR EnsemblBacteria; BAC08139; BAC08139; BAC08139.
DR KEGG; tel:tlr0587; -.
DR PATRIC; fig|197221.4.peg.620; -.
DR eggNOG; COG1600; Bacteria.
DR OrthoDB; 1478472at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0052693; F:epoxyqueuosine reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00916; QueG; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004453; QueG.
DR InterPro; IPR013542; QueG_DUF1730.
DR PANTHER; PTHR30002; PTHR30002; 1.
DR Pfam; PF08331; DUF1730; 1.
DR TIGRFAMs; TIGR00276; TIGR00276; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Queuosine biosynthesis; Reference proteome; tRNA processing.
FT CHAIN 1..312
FT /note="Epoxyqueuosine reductase"
FT /id="PRO_0000416086"
FT DOMAIN 176..203
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 183
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 209
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 237
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 240
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 244
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
SQ SEQUENCE 312 AA; 34870 MW; 7383CD4ADA581601 CRC64;
MVTAAAIKEF AHQLGFHRVG IVDLRTYTDD HPSGVAALQR WLAQGFQGEM AWMANPRRQK
IQAVLPGAKS VISVALNYYQ PDPQPPPKVK IARYAWGRDY HRVLGKRLQV LGQWLQSQVP
EMDYRWYVDT GPVQDKVWAE QAGIGWIGKH SNVISRQYGS WILLGELITT LELTGDRPHT
NHCGTCTRCL AACPTGAIVE PYVVDANRCI AYHTIESRAP ELPAAIAAHL EGWVAGCDIC
QEVCPWNQRF AQPTDVEDFA ARSPLLQTSL EELATLSDAA WDELTRGSAL RRIKSAQWRR
NAQAVLSSNP YD
