ID   TRHO_PARXL              Reviewed;         287 AA.
AC   Q142P9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=tRNA uridine(34) hydroxylase {ECO:0000255|HAMAP-Rule:MF_00469};
DE            EC=1.14.-.- {ECO:0000255|HAMAP-Rule:MF_00469};
DE   AltName: Full=tRNA hydroxylation protein O {ECO:0000255|HAMAP-Rule:MF_00469};
GN   Name=trhO {ECO:0000255|HAMAP-Rule:MF_00469}; OrderedLocusNames=Bxeno_A1152;
GN   ORFNames=Bxe_A3293;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U)
CC       modification at position 34 in tRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_00469}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA
CC         + A + H2O; Xref=Rhea:RHEA:64224, Rhea:RHEA-COMP:11727, Rhea:RHEA-
CC         COMP:13381, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:65315, ChEBI:CHEBI:136877;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00469};
CC   -!- SIMILARITY: Belongs to the TrhO family. {ECO:0000255|HAMAP-
CC       Rule:MF_00469}.
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DR   EMBL; CP000270; ABE29690.1; -; Genomic_DNA.
DR   RefSeq; WP_011487423.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q142P9; -.
DR   SMR; Q142P9; -.
DR   STRING; 266265.Bxe_A3293; -.
DR   EnsemblBacteria; ABE29690; ABE29690; Bxe_A3293.
DR   KEGG; bxb:DR64_994; -.
DR   KEGG; bxe:Bxe_A3293; -.
DR   PATRIC; fig|266265.5.peg.1185; -.
DR   eggNOG; COG1054; Bacteria.
DR   OMA; CDTHTNC; -.
DR   OrthoDB; 684577at2; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.250.10; -; 1.
DR   HAMAP; MF_00469; TrhO; 1.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR020936; TrhO.
DR   InterPro; IPR040503; TRHO_N.
DR   PANTHER; PTHR43268; PTHR43268; 1.
DR   Pfam; PF17773; UPF0176_N; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   SUPFAM; SSF54975; SSF54975; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome; tRNA processing.
FT   CHAIN           1..287
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_1000013734"
FT   DOMAIN          132..226
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        186
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   287 AA;  32108 MW;  D88E1EB29ED6E77D CRC64;
     MSIVNLSSYQ FATIEDTAAW RPFVTERCNA LGLKGTVLLA PEGINLFVAG TRENTDAFIH
     YIRHDALFEG KFADLQFKES LSDKQPFTRM LVKLKREIIT MKKPAIRPEL GRAPFVDAPT
     LKSWLDRGHD DEGRPVVMLD TRNAFEVDVG TFDNALDYRI TKFSEFPEVI EQNRADLEGK
     TIVSFCTGGI RCEKAAIHMK DVGIENVYQL EGGILKYFEE VGGAHYHGDC FVFDYRTALN
     PQLEPSKTTQ CFGCRAVVTP EAQQSPLYVA GKTCPECHPD SKAARAA