ID E8KF40_9PAST Unreviewed; 248 AA.
AC E8KF40;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Epoxyqueuosine reductase QueH {ECO:0000256|ARBA:ARBA00016895, ECO:0000256|HAMAP-Rule:MF_02089};
DE EC=1.17.99.6 {ECO:0000256|ARBA:ARBA00012622, ECO:0000256|HAMAP-Rule:MF_02089};
DE AltName: Full=Queuosine biosynthesis protein QueH {ECO:0000256|ARBA:ARBA00031446, ECO:0000256|HAMAP-Rule:MF_02089};
GN Name=queH {ECO:0000256|HAMAP-Rule:MF_02089};
GN ORFNames=HMPREF0027_0457 {ECO:0000313|EMBL:EFX92467.1};
OS Actinobacillus ureae ATCC 25976.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=887324 {ECO:0000313|EMBL:EFX92467.1, ECO:0000313|Proteomes:UP000005467};
RN [1] {ECO:0000313|EMBL:EFX92467.1, ECO:0000313|Proteomes:UP000005467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25976 {ECO:0000313|EMBL:EFX92467.1,
RC ECO:0000313|Proteomes:UP000005467};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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).
CC {ECO:0000256|ARBA:ARBA00002268, ECO:0000256|HAMAP-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:18571, Rhea:RHEA-
CC COMP:18582, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:194431, ChEBI:CHEBI:194443; EC=1.17.99.6;
CC Evidence={ECO:0000256|ARBA:ARBA00035072, ECO:0000256|HAMAP-
CC Rule:MF_02089};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004691, ECO:0000256|HAMAP-Rule:MF_02089}.
CC -!- SIMILARITY: Belongs to the QueH family. {ECO:0000256|ARBA:ARBA00008207,
CC ECO:0000256|HAMAP-Rule:MF_02089}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFX92467.1}.
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DR EMBL; AEVG01000032; EFX92467.1; -; Genomic_DNA.
DR RefSeq; WP_005621781.1; NZ_GL831080.1.
DR AlphaFoldDB; E8KF40; -.
DR HOGENOM; CLU_088177_0_0_6; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000005467; Unassembled WGS sequence.
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; EPOXYQUEUOSINE REDUCTASE QUEH; 1.
DR PANTHER; PTHR36701:SF1; EPOXYQUEUOSINE REDUCTASE QUEH; 1.
DR Pfam; PF02677; QueH; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02089};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_02089}; Iron {ECO:0000256|HAMAP-Rule:MF_02089};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02089};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02089};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02089}; Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02089};
KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_02089};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02089}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 134
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT DISULFID 217..219
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
SQ SEQUENCE 248 AA; 29557 MW; 8BFDC69D59CFFFEB CRC64;
MTEQNQQPLE HKQALQQKKK LTRKGKDPNA PFVREKLTLP SGHNKLLLHS CCAPCSGEVM
EAIHSSGIEF TIYFYNPNIH PMKEYLIRKE ENIRFAEKWG IPFIDFDDDY ENDRREWFKK
AEGMEWEPER GIRCTMCFDM RFEKAAEYAH NNGFPVYTSC LGISRWKDMN QINDCGHRAA
AKFDNVVYWD YNWRKNGGSQ RMIEISKRER FYQQEYCGCV YSLRDSNKWR LETGRQRIEI
GKLYYSPD
//
