QUEH_HAES1
ID QUEH_HAES1 Reviewed; 243 AA.
AC Q0I1Q0;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=HS_0243 {ECO:0000312|EMBL:ABI24521.1};
OS Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129Pt;
RX PubMed=17172329; DOI=10.1128/jb.01422-06;
RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA Xie G., Inzana T.J.;
RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT influenzae Rd.";
RL J. Bacteriol. 189:1890-1898(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=129Pt;
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; CP000436; ABI24521.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0I1Q0; -.
DR SMR; Q0I1Q0; -.
DR STRING; 205914.HS_0243; -.
DR EnsemblBacteria; ABI24521; ABI24521; HS_0243.
DR KEGG; hso:HS_0243; -.
DR eggNOG; COG1636; Bacteria.
DR HOGENOM; CLU_088177_0_0_6; -.
DR OMA; PNIHPYT; -.
DR UniPathway; UPA00392; -.
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..243
FT /note="Epoxyqueuosine reductase QueH"
FT /id="PRO_0000439901"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 50
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 211..213
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
SQ SEQUENCE 243 AA; 28874 MW; DD1B04C266266929 CRC64;
MHRTKLEQKQ PHFDAQKRRK KECKNSNTPF VRPKLELPHG HNKLLLHSCC APCSGEVMEA
IHASGIDFTI YFYNPNIHPL KEYLIRKEEN IRFAEKWGIP FIDADYDRQN WFDRAKGMED
EPERGIRCTM CFDMRFEKAA QYAHENGFPV FTSCLGISRW KDMNQINGCG HRAAEKYDDV
VYWDYNWRKG GGSQRMIEIS KRERFYQQEY CGCVYSLRDT NKWREANGRQ KIEIGKLYYS
ADK
