QUEG_SHEON
ID QUEG_SHEON Reviewed; 393 AA.
AC Q8EAN7;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
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=SO_3861;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(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}.
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DR EMBL; AE014299; AAN56837.1; -; Genomic_DNA.
DR RefSeq; NP_719393.1; NC_004347.2.
DR RefSeq; WP_011073619.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EAN7; -.
DR SMR; Q8EAN7; -.
DR STRING; 211586.SO_3861; -.
DR PaxDb; Q8EAN7; -.
DR KEGG; son:SO_3861; -.
DR PATRIC; fig|211586.12.peg.3748; -.
DR eggNOG; COG1600; Bacteria.
DR HOGENOM; CLU_030790_0_1_6; -.
DR OMA; ICDTDLS; -.
DR OrthoDB; 1478472at2; -.
DR PhylomeDB; Q8EAN7; -.
DR BioCyc; SONE211586:G1GMP-3583-MON; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000008186; 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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
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..393
FT /note="Epoxyqueuosine reductase"
FT /id="PRO_0000416080"
FT DOMAIN 196..228
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT ACT_SITE 154
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 208
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 211
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 214
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 218
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 234
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 261
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 264
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 268
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 393 AA; 43580 MW; 655E08247214B338 CRC64;
MSMTVTTSSN VSDAAMLSRL ALQIKSWGKA LGFAQIGICD TDLTAEEAKL QTWLDKGFHG
EMAYMETHGM MRARPHELHS GTVRVISARM DYLPPEAGFA TNLASPNMGY ISRYAGGRDY
HKLIRARLKK LGDQINSELV ALGFDAADFR PFVDSAPVLE RPLAEKAGIG WTGKHSLILN
HDAGSWFFLG ELLINLPLPV DIPVQEGCHS CVACITSCPT GAIVEPYTVD ARRCISYLTI
ELQGAIPEEF RPLMGNRIYG CDDCQLVCPV NRAAPLTQES DFHIRPKLKQ PELLTLFTWS
ETEFLKQTEG SAIRRIGHQR WLRNIAVALG NAPSSADIIS ALEQRKAQAD VDEMVKEHID
WALAQQRAGD LQTNNRKTER LVRVIQKGLP RDA
