QUEG_SYNSC
ID QUEG_SYNSC Reviewed; 321 AA.
AC Q3ANP3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
GN OrderedLocusNames=Syncc9605_0007;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000110; ABB33789.1; -; Genomic_DNA.
DR RefSeq; WP_011363051.1; NC_007516.1.
DR AlphaFoldDB; Q3ANP3; -.
DR SMR; Q3ANP3; -.
DR STRING; 110662.Syncc9605_0007; -.
DR EnsemblBacteria; ABB33789; ABB33789; Syncc9605_0007.
DR KEGG; syd:Syncc9605_0007; -.
DR eggNOG; COG1600; Bacteria.
DR HOGENOM; CLU_030790_0_0_3; -.
DR OMA; ICDTDLS; -.
DR OrthoDB; 1478472at2; -.
DR UniPathway; UPA00392; -.
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; tRNA processing.
FT CHAIN 1..321
FT /note="Epoxyqueuosine reductase"
FT /id="PRO_0000416083"
FT DOMAIN 179..211
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 191
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 194
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 197
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 201
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 217
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 245
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 248
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 252
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 321 AA; 36454 MW; 9E6F2013D1AF2269 CRC64;
MQGHVTDQQT RLSEALKRRA AEEGFNPVGI ARIPGSPRLQ LRTKALQRWL DHGHQADMAW
MAAPRRRDPR LLLDGANSVL AVGLNYYVDA QPSPGSLKVA RYGWGRDYHR VVDQRLRRIG
RWLSEQRPDC GWRACVDATP LLDKAWAEEA GLGWIGKHSN LIHPERGSWM VIGHLLTTEP
LNADPPARSL CGRCSACIDA CPTHAIREPF VVDARRCLAF HTIENREDDL PENIRAALGS
WVAGCDICQD VCPWNHRSLP QSNDPDMQPR PWLLNLHKEE IQTWDDSVWE QKLRGSALRR
IKPWMWRRNA AAAQPDPTPT L
