ID   TRHO_PROMT              Reviewed;         319 AA.
AC   Q46K33;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-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}; OrderedLocusNames=PMN2A_0654;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000095; AAZ58145.1; -; Genomic_DNA.
DR   RefSeq; WP_011294743.1; NC_007335.2.
DR   AlphaFoldDB; Q46K33; -.
DR   SMR; Q46K33; -.
DR   STRING; 59920.PMN2A_0654; -.
DR   EnsemblBacteria; AAZ58145; AAZ58145; PMN2A_0654.
DR   KEGG; pmn:PMN2A_0654; -.
DR   HOGENOM; CLU_038878_0_0_3; -.
DR   OMA; CDTHTNC; -.
DR   OrthoDB; 684577at2; -.
DR   PhylomeDB; Q46K33; -.
DR   Proteomes; UP000002535; 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; 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   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome; tRNA processing.
FT   CHAIN           1..319
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000242929"
FT   DOMAIN          133..231
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        191
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   319 AA;  36459 MW;  005E515CE7360B55 CRC64;
     MKKDDRLKKF KYKVAAFYNF ISIIDEEILL IKEELTKLAT NQKIKGTILL ASEGVNGTIC
     GPENAIVQFI ETLEKLLKVS DINVKYSWSE KQAFRRFKAR KKKEIVTIGL KEINPTKSVG
     KYIKAGEWNQ FLEDPNSVVI DTRNEYEIKI GNFAGALNPQ TSSFREFPAW VQKHLKPLIE
     ENPSLKIGMY CTGGIRCEKA TSYLIEEGFS DVHHLEGGIL KYLEDVSSEN SLWNGECFVF
     DQRVSLDHEL LPGSHRMCHA CGLPISPEDL KKPTYIKGLQ CDACVNKFTD SDRARFAERQ
     RQIDEIMKRL PENSIWPSS