ID   TRHO_CYTH3              Reviewed;         312 AA.
AC   Q11RM1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=CHU_2691;
OS   Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS   15051 / NCIMB 9469 / D465).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Cytophaga.
OX   NCBI_TaxID=269798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX   PubMed=17400776; DOI=10.1128/aem.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA   Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA   Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA   McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(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; CP000383; ABG59943.1; -; Genomic_DNA.
DR   RefSeq; WP_011586053.1; NZ_FPJX01000002.1.
DR   AlphaFoldDB; Q11RM1; -.
DR   SMR; Q11RM1; -.
DR   STRING; 269798.CHU_2691; -.
DR   PRIDE; Q11RM1; -.
DR   EnsemblBacteria; ABG59943; ABG59943; CHU_2691.
DR   KEGG; chu:CHU_2691; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_1_0_10; -.
DR   OMA; CDTHTNC; -.
DR   OrthoDB; 684577at2; -.
DR   Proteomes; UP000001822; 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   PANTHER; PTHR43268; PTHR43268; 1.
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; Reference proteome; tRNA processing.
FT   CHAIN           1..312
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_1000081187"
FT   DOMAIN          123..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   312 AA;  35553 MW;  C83943F28491F5B5 CRC64;
     MKDYQILLYY CYTHIADPDA YREEHHLKCL ELGLLGRIII ASEGLNGTVS GTEEGCRQYM
     EYVKADPRFE ALEFKIEAHE GHAFQKLYVR VKPEIVHSSL KHVDPTKRTG KHLEPAEFKA
     MKDRDDVVVL DVRSNYEHQV GRFKNAVTID MENFRDFPEK IKELDHLKGK KVLTYCTGGI
     KCEKASAFLL EQGFEDVYQL HGGIIKYGIE QGGEDFEGKC YVFDGRVIAD VNKVNPSIIS
     TCYVCGTLSD RMVNCSNPVC NRHEPMCEAC GEKMQGACSE ECKCHPEKRP YDGTGAYPKE
     LNGYDPYLHV KR