QUEG_BACCR
ID QUEG_BACCR Reviewed; 380 AA.
AC Q81I72;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=BC_0544;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP07564.1; -; Genomic_DNA.
DR RefSeq; NP_830363.1; NC_004722.1.
DR RefSeq; WP_000345215.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81I72; -.
DR SMR; Q81I72; -.
DR STRING; 226900.BC_0544; -.
DR EnsemblBacteria; AAP07564; AAP07564; BC_0544.
DR GeneID; 67505241; -.
DR KEGG; bce:BC0544; -.
DR PATRIC; fig|226900.8.peg.500; -.
DR HOGENOM; CLU_030790_2_0_9; -.
DR OMA; ICDTDLS; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001417; 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 Gene3D; 1.25.10.10; -; 1.
DR HAMAP; MF_00916; QueG; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR InterPro; IPR004453; QueG.
DR InterPro; IPR013542; QueG_DUF1730.
DR PANTHER; PTHR30002; PTHR30002; 1.
DR Pfam; PF08331; DUF1730; 1.
DR SMART; SM00567; EZ_HEAT; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR TIGRFAMs; TIGR00276; TIGR00276; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Queuosine biosynthesis; Reference proteome; Repeat; tRNA processing.
FT CHAIN 1..380
FT /note="Epoxyqueuosine reductase"
FT /id="PRO_0000416065"
FT DOMAIN 178..208
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT DOMAIN 226..258
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT BINDING 188
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 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 198
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 214
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 243
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 247
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 380 AA; 42398 MW; 551F430DDE70E409 CRC64;
MDFEQLKQDV IAYSKTIGID KIGFASASPF EELKQRLIQQ QQLNYQSGFE EPDIEKRTNP
QLLLPGAKSI IAIALAYPSK LKNAPLSKRG ERRGIFCRAS WGQDYHLVLR DRLQKLEAYL
IEKLPDIEVK SMVDTGELSD RAVSERAGIG WSGKNCSIIT PEFGSYVYLG EMITNVPFPP
DKPIEDQCGG CTKCIDICPT GALIQGGQLD SKKCIAFLTQ TKGFLPEEYR DKIGNRIYGC
DTCQTVCPKN KGMDFHNHPE MEPDPELVKP LLTPLLTISN RDFKEKYGIM SGSWRGKKPL
QRNAILALAH FKEASAIPDL IGVMKDDPRP VLRGTAAWAL GKIGGDGVGE AIEKAMEREK
DEEVLHEMNR GLELLAQKKE
