ID   TRHO_PSEAB              Reviewed;         312 AA.
AC   Q02I17;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=PA14_53180;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ10017.1; -; Genomic_DNA.
DR   RefSeq; WP_003140843.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02I17; -.
DR   SMR; Q02I17; -.
DR   PRIDE; Q02I17; -.
DR   EnsemblBacteria; ABJ10017; ABJ10017; PA14_53180.
DR   KEGG; pau:PA14_53180; -.
DR   HOGENOM; CLU_038878_0_0_6; -.
DR   OMA; CDTHTNC; -.
DR   BioCyc; PAER208963:G1G74-4475-MON; -.
DR   Proteomes; UP000000653; Chromosome.
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; 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; PF00581; Rhodanese; 1.
DR   Pfam; PF17773; UPF0176_N; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; tRNA processing.
FT   CHAIN           1..312
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_1000013758"
FT   DOMAIN          123..217
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   REGION          282..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        177
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   312 AA;  35464 MW;  32DEDCFD2D7A1E93 CRC64;
     MTSIVVAALY KFVTLDDYVA LREPLLQTLL DNGVKGTLLL AEEGINGTVS GSREGIDALF
     AWLRSDPRLA DIEHKESYCD EQPFYRTKVK LKKEIVTLGV LGVDPNKQVG QYVEAKDWNA
     LISDPEVLLI DTRNDYEVAI GTFEGAVDPK TRSFREFPEY IKAHYDPARH KKVAMFCTGG
     IRCEKASSYM LGAGFEEVFH LRGGILKYLE EVPQEQSLWR GDCFVFDNRV TVRHDLSEGE
     YDQCHACRNP VSLEDRQSEH YVPGISCPHC WDSLSEKTRA GARERQKQIE LARQRNQPHP
     LGRDPRQSTL EN