QUEH_STAES
ID QUEH_STAES Reviewed; 238 AA.
AC A0A0H2VKG8;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Epoxyqueuosine reductase QueH {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000303|PubMed:28128549};
DE EC=1.17.99.6 {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000305|PubMed:28128549};
DE AltName: Full=Queuosine biosynthesis protein QueH {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000305};
GN Name=queH {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000303|PubMed:28128549};
GN OrderedLocusNames=SE_2135 {ECO:0000312|EMBL:AAO05777.1};
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=28128549; DOI=10.1021/acschembio.6b01100;
RA Zallot R., Ross R., Chen W.H., Bruner S.D., Limbach P.A.,
RA de Crecy-Lagard V.;
RT "Identification of a novel epoxyqueuosine reductase family by comparative
RT genomics.";
RL ACS Chem. Biol. 12:844-851(2017).
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_02089, ECO:0000269|PubMed:28128549}.
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_02089,
CC ECO:0000305|PubMed:28128549};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000305|PubMed:28128549}.
CC -!- SIMILARITY: Belongs to the QueH family. {ECO:0000255|HAMAP-
CC Rule:MF_02089, ECO:0000305}.
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DR EMBL; AE015929; AAO05777.1; -; Genomic_DNA.
DR RefSeq; NP_765690.1; NC_004461.1.
DR RefSeq; WP_002485460.1; NZ_WBME01000005.1.
DR AlphaFoldDB; A0A0H2VKG8; -.
DR SMR; A0A0H2VKG8; -.
DR STRING; 176280.SE_2135; -.
DR EnsemblBacteria; AAO05777; AAO05777; SE_2135.
DR KEGG; sep:SE_2135; -.
DR PATRIC; fig|176280.10.peg.2086; -.
DR eggNOG; COG1636; Bacteria.
DR HOGENOM; CLU_088177_1_0_9; -.
DR OMA; PNIHPYT; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001411; 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 HAMAP; MF_02089; QueH; 1.
DR InterPro; IPR003828; QueH.
DR PANTHER; PTHR36701; PTHR36701; 1.
DR Pfam; PF02677; QueH; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Disulfide bond; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Queuosine biosynthesis; Redox-active center; tRNA processing.
FT CHAIN 1..238
FT /note="Epoxyqueuosine reductase QueH"
FT /id="PRO_0000439904"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT DISULFID 211..213
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
SQ SEQUENCE 238 AA; 27578 MW; 8F98CD29BF011F65 CRC64;
MIEANQILAK MKNQKINYDK VLRKIISQWE RDGERPKILL HSCCAPCSTY TLEFLTQYAD
IAIYFANPNI HPKSEYLRRA KVQEQFVNDF NNKTGASVKY IEAEYEPHKF MKMAKDKGLT
EEPEGGLRCT ACFEMRLEIV AKAALEHGYD YFGSAITLSP KKNAQLINEL GMDVQNIYNV
KYLPSDFKKN KGYERSIEMC NDYNIFRQCY CGCVFAAMKQ GIDFKQINKD AQAFLQQF
