QUEH_THEMA
ID QUEH_THEMA Reviewed; 192 AA.
AC Q9WZJ0;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=TM_0731 {ECO:0000312|EMBL:AAD35833.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD35833.1; -; Genomic_DNA.
DR PIR; F72338; F72338.
DR RefSeq; NP_228540.1; NC_000853.1.
DR PDB; 7LC5; X-ray; 1.50 A; A=1-192.
DR PDB; 7LC7; X-ray; 1.58 A; A=1-192.
DR PDBsum; 7LC5; -.
DR PDBsum; 7LC7; -.
DR AlphaFoldDB; Q9WZJ0; -.
DR SMR; Q9WZJ0; -.
DR STRING; 243274.THEMA_01000; -.
DR EnsemblBacteria; AAD35833; AAD35833; TM_0731.
DR KEGG; tma:TM0731; -.
DR PATRIC; fig|243274.5.peg.744; -.
DR eggNOG; COG1636; Bacteria.
DR InParanoid; Q9WZJ0; -.
DR OMA; PNIHPYT; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000008183; 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 3D-structure; 4Fe-4S; Disulfide bond; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Queuosine biosynthesis; Redox-active center;
KW Reference proteome; tRNA processing.
FT CHAIN 1..192
FT /note="Epoxyqueuosine reductase QueH"
FT /id="PRO_0000439906"
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 10
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT DISULFID 169..171
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:7LC5"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:7LC5"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:7LC5"
FT HELIX 36..53
FT /evidence="ECO:0007829|PDB:7LC5"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7LC5"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:7LC5"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:7LC5"
FT HELIX 85..104
FT /evidence="ECO:0007829|PDB:7LC5"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:7LC5"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:7LC5"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7LC7"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:7LC5"
FT TURN 145..149
FT /evidence="ECO:0007829|PDB:7LC5"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:7LC5"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:7LC5"
SQ SEQUENCE 192 AA; 22509 MW; 78F78856FDBB3122 CRC64;
MGTVLIHVCC APDLLTTIFH VRDAEFFFYN PNIQPLSEYE KRREAVDKVA NHFSLNVRYG
EYSTEEIRKW YTAVKDYKDL GEGSKRCERC ISFLLERTAQ EARKRGHESF STTLLASPRK
NLPMIENIGK TIEEKYGVKF FFKNFRKGGA YQEGVRLSKE LGIYRQNYCG CVFSLLERRE
KHAEISRKRG HM
