ID A0A0Q6MB08_9BURK Unreviewed; 365 AA.
AC A0A0Q6MB08;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=ASC88_27140 {ECO:0000313|EMBL:KQU74619.1};
OS Rhizobacter sp. Root29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU74619.1, ECO:0000313|Proteomes:UP000051195};
RN [1] {ECO:0000313|EMBL:KQU74619.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU74619.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU74619.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU74619.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQU74619.1}.
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DR EMBL; LMCN01000017; KQU74619.1; -; Genomic_DNA.
DR RefSeq; WP_056806455.1; NZ_LMCN01000017.1.
DR AlphaFoldDB; A0A0Q6MB08; -.
DR STRING; 1736511.ASC88_27140; -.
DR OrthoDB; 9784571at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000051195; Unassembled WGS sequence.
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|ARBA:ARBA00022485, 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}; Reference proteome {ECO:0000313|Proteomes:UP000051195};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00916}.
FT DOMAIN 190..221
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT BINDING 64
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT BINDING 147
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT BINDING 182
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT BINDING 201
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 204
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 207
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 211
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 227
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 229
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT BINDING 254..255
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT BINDING 254
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 257
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 261
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 365 AA; 40061 MW; 9A6AD4C0F21EA177 CRC64;
MTEAQQVDGD GLVAQLREWG LALGFSQIGV ADVDLSSAEA GLLAWLRDGF HGEMGYMAAH
GLKRARPAEL VPGTVRVITA RMDYLPKDTA DDWQAVEWQR LASPAQAAVS VYARGRDYHK
VLRNRLQKLA DRLQQAVGPR GHRVFTDSAP VLEVELASRS GIGWRGKHTL TLHREAGSMF
FLGEIYVDLP LPLSTPVTGH CGSCSACIDV CPTRAIVAPY RVDARRCISY LTIEHAGPIP
VELRPALGNR IYGCDDCQLA CPWNKYAQRS PLPDFDLRDA LATPTLLGLW AWTEADFLRH
TEGSAIRRIG HQRWRRNLAV AIGNALRHAA TPAADRAALA AALQASREGA DELVREHIDW
ALSEA
//
