QUEH_STRP1
ID QUEH_STRP1 Reviewed; 255 AA.
AC Q9A1K3; Q491A1;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=SPy_0233 {ECO:0000312|EMBL:AAK33314.1};
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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; AE004092; AAK33314.1; -; Genomic_DNA.
DR RefSeq; NP_268593.1; NC_002737.2.
DR AlphaFoldDB; Q9A1K3; -.
DR SMR; Q9A1K3; -.
DR STRING; 1314.HKU360_00239; -.
DR PaxDb; Q9A1K3; -.
DR EnsemblBacteria; AAK33314; AAK33314; SPy_0233.
DR KEGG; spy:SPy_0233; -.
DR PATRIC; fig|160490.10.peg.206; -.
DR HOGENOM; CLU_088177_1_0_9; -.
DR OMA; PNIHPYT; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000000750; 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; Reference proteome;
KW tRNA processing.
FT CHAIN 1..255
FT /note="Epoxyqueuosine reductase QueH"
FT /id="PRO_0000439905"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT DISULFID 210..212
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
SQ SEQUENCE 255 AA; 29724 MW; 850A594C158CA329 CRC64;
MIDLQEILAN MNPNQKINYD RVMQQMAKVW EKESVRPSIL MHVCCAPCST YTLEYLTQFA
DITVYFANSN IHPKDEYHRR AYVTQQFVSE FNAKTGNTVQ FLEADYVPNE YVRQVRGLEE
EPEGGDRCRV CFDYRLDKTA QKAVELGFDY FASALTISPH KNSQTINDVG IDVQKVYTTK
YLPSDFKKNN GYRRSVEMCE EYDIYRQCYC GCVYAAKMQG IDLVQVKKDA KAFMADKDLD
NDFTHIRFSY RGDEM
