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TRHO_SYNY3
ID   TRHO_SYNY3              Reviewed;         278 AA.
AC   Q55613;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=sll0765;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA10124.1; -; Genomic_DNA.
DR   PIR; S76272; S76272.
DR   AlphaFoldDB; Q55613; -.
DR   SMR; Q55613; -.
DR   STRING; 1148.1001499; -.
DR   PaxDb; Q55613; -.
DR   EnsemblBacteria; BAA10124; BAA10124; BAA10124.
DR   KEGG; syn:sll0765; -.
DR   eggNOG; COG1054; Bacteria.
DR   InParanoid; Q55613; -.
DR   OMA; CDTHTNC; -.
DR   PhylomeDB; Q55613; -.
DR   Proteomes; UP000001425; 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..278
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000161533"
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   278 AA;  31166 MW;  FA9E085AC41452AB CRC64;
     MAYQVTTFYH FTRLNCLAEK QSRWQELGDR LGLKGTILLA EEGVNATIAG ESAAIEEMVK
     IMAADLGLTS VPQRHSWAKT IPFQRMKVKI KPEIVSLGQP QVNPEKQVGT YVSPQQWNQL
     LQDPDVVVID TRNDYEVAIG TFQGAVNPCT KKFRQFPDYV KNNLDQQKNK KVAMFCTGGI
     RCEKASAYLL EEGFAEVYHL RGGILHYLET IAPEESLWQG ECFVFDERVA VQEGLKVGSH
     ALCDHCGYPL RVGDLAEIRY AVRHCPQCGL TVAVSNEL
 
 
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