ID   TRHO_ECOL6              Reviewed;         350 AA.
AC   Q8FIR7;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 2.
DT   25-MAY-2022, entry version 85.
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=c1321;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U)
CC       modification at position 34 in tRNAs, the first step in 5-
CC       carboxymethoxyuridine (cmo5U) biosynthesis. May be part of an alternate
CC       pathway, which is able to bypass cmo5U biogenesis in a subset of tRNAs
CC       under aerobic conditions. {ECO:0000250|UniProtKB:P24188}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79794.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN79794.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001298360.1; NC_004431.1.
DR   AlphaFoldDB; Q8FIR7; -.
DR   SMR; Q8FIR7; -.
DR   STRING; 199310.c1321; -.
DR   EnsemblBacteria; AAN79794; AAN79794; c1321.
DR   KEGG; ecc:c1321; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_1_1_6; -.
DR   OMA; CDTHTNC; -.
DR   Proteomes; UP000001410; 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_0000161471"
FT   DOMAIN          146..240
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        200
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   350 AA;  39735 MW;  9AAE1F14C76F574E CRC64;
     MPVLHNRISN DALKAKMLAE SEPRTTISFY KYFHIADPKV TRDALYQLFT ALNVFGRVYL
     AHEGINAQIS VPASNVETFR AQLYAFDPAL EGLRLNIALD DDGKSFWVLR MKVRDRIVAD
     GIDDPHFDAS NVGEYLQAAE VNAMLDDPDA LFIDMRNHYE YEVGHFENAL EIPADTFREQ
     LPKAVEMMQA HKDKKIVMYC TGGIRCEKAS AWMKHNGFNK VWHIEGGIIE YARKARDQGL
     PVRFIGKNFV FDERMGERIS DEIIAHCHQC GAPCDSHTNC KNDGCHLLFI QCPVCAEKYK
     GCCSEICCEE SALPPDEQRR RRAGRENGNK IFNKSRGRLN TTLGIPDPTE