QUEH_HAEIN
ID QUEH_HAEIN Reviewed; 245 AA.
AC P44068;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Epoxyqueuosine reductase QueH {ECO:0000255|HAMAP-Rule:MF_02089};
DE EC=1.17.99.6 {ECO:0000255|HAMAP-Rule:MF_02089};
DE AltName: Full=Queuosine biosynthesis protein QueH {ECO:0000255|HAMAP-Rule:MF_02089};
GN Name=queH {ECO:0000255|HAMAP-Rule:MF_02089}; OrderedLocusNames=HI_0882;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
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}.
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 -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02089}.
CC -!- SIMILARITY: Belongs to the QueH family. {ECO:0000255|HAMAP-
CC Rule:MF_02089}.
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DR EMBL; L42023; AAC22546.1; -; Genomic_DNA.
DR PIR; E64015; E64015.
DR RefSeq; NP_439043.1; NC_000907.1.
DR RefSeq; WP_005651413.1; NC_000907.1.
DR AlphaFoldDB; P44068; -.
DR SMR; P44068; -.
DR STRING; 71421.HI_0882; -.
DR PRIDE; P44068; -.
DR EnsemblBacteria; AAC22546; AAC22546; HI_0882.
DR KEGG; hin:HI_0882; -.
DR PATRIC; fig|71421.8.peg.924; -.
DR eggNOG; COG1636; Bacteria.
DR HOGENOM; CLU_088177_0_0_6; -.
DR OMA; PNIHPYT; -.
DR PhylomeDB; P44068; -.
DR BioCyc; HINF71421:G1GJ1-922-MON; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000000579; 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..245
FT /note="Epoxyqueuosine reductase QueH"
FT /id="PRO_0000077968"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT BINDING 53
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 BINDING 134
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
FT DISULFID 214..216
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089"
SQ SEQUENCE 245 AA; 29072 MW; BC55B4EB8ED65491 CRC64;
MNTELQPKLE KSAVNFQAKP RKQKIRKDPN APFIREKLEL PDGHNKLLLH SCCAPCSGEV
MEAILASGIE FTIYFYNPNI HPLKEYLIRK EENIRFAKKF GIPFIDADYD RQNWFDRAKG
MEWEPERGIR CTMCFDMRFE KAAEYAHKHG FPVFTSCLGI SRWKDMNQIN GCGHRAAEKY
DDVIYWDYNW RKEGGSQRMI EISKRERFYQ QEYCGCVYSL RDSNKWREET GRQKIEIGKL
YYSAD
