ID   TRHO_SYNE7              Reviewed;         269 AA.
AC   Q31LZ7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
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};
GN   OrderedLocusNames=Synpcc7942_1892;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; CP000100; ABB57922.1; -; Genomic_DNA.
DR   RefSeq; WP_011244513.1; NC_007604.1.
DR   AlphaFoldDB; Q31LZ7; -.
DR   SMR; Q31LZ7; -.
DR   STRING; 1140.Synpcc7942_1892; -.
DR   PRIDE; Q31LZ7; -.
DR   EnsemblBacteria; ABB57922; ABB57922; Synpcc7942_1892.
DR   KEGG; syf:Synpcc7942_1892; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_0_1_3; -.
DR   OMA; CDTHTNC; -.
DR   OrthoDB; 684577at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1892-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; IPR036046; Acylphosphatase-like_dom_sf.
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   SUPFAM; SSF54975; SSF54975; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; tRNA processing.
FT   CHAIN           1..269
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000242953"
FT   DOMAIN          122..216
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        176
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   269 AA;  29967 MW;  46C61372F3434049 CRC64;
     MSLVLINFYR FVALGDCDRW RQWLQDLCTA LGLRGTILLA PEGINAGLAG NTEAIAQFLS
     ELQQHPPFAN LSFKSATVTD WPFARLKVKV KPEIVSLGCP ELNPAERTGT LVAPQDWNQL
     LQDPEVVLID VRNRFEIALG SFPRAIDPQT DRFRDFPRFV QEQLLPQPPA KVAMFCTGGI
     RCEKASAYLL EQGIETVYQL EGGILNYLEA IAPEENHWQG DCFVFDERIA VDRQLQTPQH
     QLCPACGQPV VATTCSHCQD SVQASSSPK