ID   TRHO_SHIF8              Reviewed;         350 AA.
AC   Q0T5X6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=SFV_1078;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(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; CP000266; ABF03289.1; -; Genomic_DNA.
DR   RefSeq; WP_001144616.1; NC_008258.1.
DR   AlphaFoldDB; Q0T5X6; -.
DR   SMR; Q0T5X6; -.
DR   EnsemblBacteria; ABF03289; ABF03289; SFV_1078.
DR   GeneID; 66670678; -.
DR   KEGG; sfv:SFV_1078; -.
DR   HOGENOM; CLU_038878_1_1_6; -.
DR   OMA; CDTHTNC; -.
DR   BioCyc; SFLE373384:SFV_RS05975-MON; -.
DR   Proteomes; UP000000659; 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_1000013778"
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;  61AB5F317B0C24DB CRC64;
     MPVLHNRISN DALKAKMLAE SEPRTTISFY KYFHIADPKA TRDALYQLFT ALNVFGRVYL
     AHEGINAQIS VPASNVETFR AQLYAFDPAL EGLRLNIALD DDGKSFWVLR MKVRDRIVAD
     GIDDPHFDAS NVGEYLQAAE VNAMLDDPDA LFIDMRNHYE YEVGHFENAL EIPADTFREQ
     LPKAVEMMQA HKDKKIVMYC TGGIRCEKAS AWMKHNGFNK VWHIEGGIIE YARKAREQGL
     PVRFIGKNFV FDERMGERIS DEIIAHCHQC GAPCDSHTNC KNDGCHLLFI QCPVCAEKYK
     GCCSEICCEE SALPPEEQRR RRAGRENGNK IFNKSRGRLN TTLGIPDPTE