ID   TRHO_YERPB              Reviewed;         355 AA.
AC   B2K776;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=YPTS_2579;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001048; ACC89539.1; -; Genomic_DNA.
DR   RefSeq; WP_002211854.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2K776; -.
DR   SMR; B2K776; -.
DR   GeneID; 66845088; -.
DR   KEGG; ypb:YPTS_2579; -.
DR   PATRIC; fig|502801.10.peg.1989; -.
DR   OMA; CDTHTNC; -.
DR   BioCyc; YPSE502801:YPTS_RS12985-MON; -.
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..355
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_1000200390"
FT   DOMAIN          146..240
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   REGION          333..355
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   355 AA;  40550 MW;  3F9C2BACC80A44FC CRC64;
     MPVLHNRISN EELKARMLAE TEPRTTVSFY KYFTLEDAKT FRDNLYSQFV KLGVFGRVYV
     AKEGINAQIS VPANRYDEFK IALFASHPAL DQVRLNVAHE DDGKSFWVLR LKVRERIVAD
     GIDDDSFDPA NIGHYLKADQ VNQMIDDPDT LFVDMRNHYE YEVGHFENAI EVPSDTFREQ
     LPMAVDMLQH DKEKNIVMYC TGGIRCEKAS AYMLHNGFKN VYHVEGGIIE YARKAKEQGL
     PLKFIGKNFV FDERMGERIS DDVIAHCHQC GTPCDAHTNC KNDGCHLLFI QCPVCAAKFE
     GCCSQICQEE LKLPQEEQRS RRAGRENGIK IFNKSKGLLQ ATMHIPSPEK SADEK