ID   TRHO_SALCH              Reviewed;         350 AA.
AC   Q57QK2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 73.
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}; Synonyms=yceA;
GN   OrderedLocusNames=SCH_1103;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX65009.1; -; Genomic_DNA.
DR   RefSeq; WP_001144626.1; NC_006905.1.
DR   AlphaFoldDB; Q57QK2; -.
DR   SMR; Q57QK2; -.
DR   EnsemblBacteria; AAX65009; AAX65009; SCH_1103.
DR   KEGG; sec:SCH_1103; -.
DR   HOGENOM; CLU_038878_1_1_6; -.
DR   OMA; CDTHTNC; -.
DR   Proteomes; UP000000538; 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; IPR022111; Rhodanese_C.
DR   InterPro; IPR020936; TrhO.
DR   InterPro; IPR040503; TRHO_N.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF12368; Rhodanese_C; 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..350
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000161507"
FT   DOMAIN          146..240
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   REGION          319..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        200
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   350 AA;  39939 MW;  1B5999052E8243A9 CRC64;
     MPVLHNRISN DELKAKMLAE SEPRTTISFY KYFTIASPQQ TRDALYQVFT ALDVFGRVYL
     AHEGINAQIS VPQSKLETFR QQLYTFDPAL DGLRLNIALE DDGKSFWVLR MKVRDRIVAD
     GIDDPSFDAS NVGDYLKAAD VNVMLDDPDA VFIDMRNHYE YEVGHFENAL EIPADTFREQ
     LPKAVEMLRE HADKKIVMYC TGGIRCEKAS AWMKHNGFNK VWHIEGGIIE YARRAREQGL
     PVRFIGKNFV FDERMGERIS DEVIAHCHQC GASCDSHTNC KNDGCHLLFI QCPQCASKFN
     GCCSEQCCEE LALPEEEQRR RRAGRENGNK IFNKSRGRLN SKLSIPDPAE