ID D4H2P8_DENA2 Unreviewed; 192 AA.
AC D4H2P8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Epoxyqueuosine reductase QueH {ECO:0000256|ARBA:ARBA00016895, ECO:0000256|HAMAP-Rule:MF_02089};
DE EC=1.17.99.6 {ECO:0000256|ARBA:ARBA00012622, ECO:0000256|HAMAP-Rule:MF_02089};
DE AltName: Full=Queuosine biosynthesis protein QueH {ECO:0000256|ARBA:ARBA00031446, ECO:0000256|HAMAP-Rule:MF_02089};
GN Name=queH {ECO:0000256|HAMAP-Rule:MF_02089};
GN OrderedLocusNames=Dacet_0309 {ECO:0000313|EMBL:ADD67109.1};
OS Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Geovibrionaceae; Denitrovibrio.
OX NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67109.1, ECO:0000313|Proteomes:UP000002012};
RN [1] {ECO:0000313|EMBL:ADD67109.1, ECO:0000313|Proteomes:UP000002012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12809 / NBRC 114555 / N2460
RC {ECO:0000313|Proteomes:UP000002012};
RX PubMed=21304711; DOI=10.4056/sigs.892105;
RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT (N2460).";
RL Stand. Genomic Sci. 2:270-279(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).
CC {ECO:0000256|ARBA:ARBA00002268, ECO:0000256|HAMAP-Rule:MF_02089}.
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|ARBA:ARBA00035072, ECO:0000256|HAMAP-
CC Rule:MF_02089};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004691, ECO:0000256|HAMAP-Rule:MF_02089}.
CC -!- SIMILARITY: Belongs to the QueH family. {ECO:0000256|ARBA:ARBA00008207,
CC ECO:0000256|HAMAP-Rule:MF_02089}.
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DR EMBL; CP001968; ADD67109.1; -; Genomic_DNA.
DR RefSeq; WP_013009654.1; NC_013943.1.
DR AlphaFoldDB; D4H2P8; -.
DR STRING; 522772.Dacet_0309; -.
DR PaxDb; 522772-Dacet_0309; -.
DR KEGG; dap:Dacet_0309; -.
DR eggNOG; COG1636; Bacteria.
DR HOGENOM; CLU_088177_1_1_0; -.
DR InParanoid; D4H2P8; -.
DR OrthoDB; 9801033at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000002012; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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 CDD; cd01986; Alpha_ANH_like; 1.
DR HAMAP; MF_02089; QueH; 1.
DR InterPro; IPR003828; QueH.
DR PANTHER; PTHR36701; EPOXYQUEUOSINE REDUCTASE QUEH; 1.
DR PANTHER; PTHR36701:SF1; EPOXYQUEUOSINE REDUCTASE QUEH; 1.
DR Pfam; PF02677; QueH; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02089};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_02089}; Iron {ECO:0000256|HAMAP-Rule:MF_02089};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02089};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02089};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02089}; Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02089};
KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_02089};
KW Reference proteome {ECO:0000313|Proteomes:UP000002012};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02089}.
FT BINDING 8
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT DISULFID 163..165
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
SQ SEQUENCE 192 AA; 23189 MW; 86289C295492C6F2 CRC64;
MKILLHQCCG PCSVYPVRVL KEQGHSIMGY WFNPNIHPVT EYYKRLETLR KFNDDESLKT
IIDETYGLTE FTRSASFRED ARCRYCYQVR IENTAQIASR GKFDAFTTTL MYSRWQDHEL
MKEFCELAAK KYKIIFHYED YRTGWQEGIE TSKKRGMYRQ QYCGCIYSEE ERYRQQLSKR
FAEGKEIREF LK
//
