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Database: UniProt
Entry: E1SFL1_PANVC
LinkDB: E1SFL1_PANVC
Original site: E1SFL1_PANVC 
ID   E1SFL1_PANVC            Unreviewed;       379 AA.
AC   E1SFL1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Epoxyqueuosine reductase {ECO:0000256|HAMAP-Rule:MF_00916};
DE            EC=1.17.99.6 {ECO:0000256|HAMAP-Rule:MF_00916};
DE   AltName: Full=Queuosine biosynthesis protein QueG {ECO:0000256|HAMAP-Rule:MF_00916};
GN   Name=queG {ECO:0000256|HAMAP-Rule:MF_00916};
GN   Synonyms=yjeS {ECO:0000313|EMBL:ADO10957.1};
GN   OrderedLocusNames=Pvag_2798 {ECO:0000313|EMBL:ADO10957.1};
OS   Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO10957.1, ECO:0000313|Proteomes:UP000006631};
RN   [1] {ECO:0000313|EMBL:ADO10957.1, ECO:0000313|Proteomes:UP000006631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C9-1 {ECO:0000313|EMBL:ADO10957.1,
RC   ECO:0000313|Proteomes:UP000006631};
RX   PubMed=20952567; DOI=10.1128/JB.01122-10;
RA   Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA   Stockwell V.O., Frey J.E., Duffy B.;
RT   "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL   J. Bacteriol. 192:6486-6487(2010).
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:0000256|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:18571, Rhea:RHEA-
CC         COMP:18582, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:194431, ChEBI:CHEBI:194443; EC=1.17.99.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00916};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00916};
CC       Note=Binds 2 [4Fe-4S] clusters per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00916};
CC   -!- COFACTOR:
CC       Name=cob(II)alamin; Xref=ChEBI:CHEBI:16304;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00916};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00916}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00916}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00916}.
CC   -!- SIMILARITY: Belongs to the QueG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00916}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00916}.
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DR   EMBL; CP002206; ADO10957.1; -; Genomic_DNA.
DR   RefSeq; WP_013359187.1; NC_014562.1.
DR   AlphaFoldDB; E1SFL1; -.
DR   KEGG; pva:Pvag_2798; -.
DR   eggNOG; COG1600; Bacteria.
DR   HOGENOM; CLU_030790_0_1_6; -.
DR   OMA; FPAPYQL; -.
DR   OrthoDB; 9784571at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000006631; 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:0031419; F:cobalamin 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   Gene3D; 3.30.70.20; -; 1.
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   NCBIfam; TIGR00276; tRNA epoxyqueuosine(34) reductase QueG; 1.
DR   PANTHER; PTHR30002; EPOXYQUEUOSINE REDUCTASE; 1.
DR   PANTHER; PTHR30002:SF4; EPOXYQUEUOSINE REDUCTASE; 1.
DR   Pfam; PF13484; Fer4_16; 1.
DR   Pfam; PF08331; QueG_DUF1730; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Cobalamin {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00916};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00916};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00916};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00916}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00916};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00916}.
FT   DOMAIN          181..213
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   ACT_SITE        139
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         62
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         139
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         157
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         163
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         174
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         193
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         196
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         199
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         203
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         219
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         221
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         246..247
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         246
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         249
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         253
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
SQ   SEQUENCE   379 AA;  43327 MW;  88FD9D47735F4861 CRC64;
     MSYPLDLHEL AQQIKQWGLD LGFQQVGITD TDLSAEEPRL QEWLDKQYHG EMAWMARHGM
     MRARAHELLP GTLRVISVRM NYLPAKAAFA STLKNPRLGY VSRYALGRDY HKVLRNRLKK
     LGEMIQQHCG ELNFRPFVDS APLLERPLAA KAGLGWTGKH SLILNREAGS WFFLGELLID
     IPLPVDSPQQ EQCGRCVACM TICPTSAIVE PYVVDARRCI SYLTIELEGA IPEEFRPLMG
     NRIYGCDDCQ LICPWNRYGQ LSDESDFSPR AALHAPELLD LFQWDEAKFL RITEGSAIRR
     IGHLRWLRNI AVALGNAPWS PHIIHVLEQR LGESELLDEH IQWAVMQQQQ KREQLVVEVQ
     PAQQKRLVRA VEKGLPRDA
//
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