TRHO_SHIFL
ID TRHO_SHIFL Reviewed; 350 AA.
AC Q83LJ0; Q7UCX7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 4.
DT 25-MAY-2022, entry version 106.
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}; Synonyms=yceA;
GN OrderedLocusNames=SF1062, S1139;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42684.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16570.1; -; Genomic_DNA.
DR RefSeq; NP_706977.2; NC_004337.2.
DR RefSeq; WP_001144616.1; NZ_WPGW01000001.1.
DR AlphaFoldDB; Q83LJ0; -.
DR SMR; Q83LJ0; -.
DR STRING; 198214.SF1062; -.
DR DNASU; 1077536; -.
DR EnsemblBacteria; AAN42684; AAN42684; SF1062.
DR EnsemblBacteria; AAP16570; AAP16570; S1139.
DR GeneID; 1026260; -.
DR GeneID; 66670678; -.
DR KEGG; sfl:SF1062; -.
DR KEGG; sfx:S1139; -.
DR PATRIC; fig|198214.7.peg.1243; -.
DR HOGENOM; CLU_038878_1_1_6; -.
DR OMA; CDTHTNC; -.
DR OrthoDB; 684577at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 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..350
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_1000013779"
FT DOMAIN 146..240
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT ACT_SITE 200
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 350 AA; 39735 MW; 61AB5F317B0C24DB CRC64;
MPVLHNRISN DALKAKMLAE SEPRTTISFY KYFHIADPKA TRDALYQLFT ALNVFGRVYL
AHEGINAQIS VPASNVETFR AQLYAFDPAL EGLRLNIALD DDGKSFWVLR MKVRDRIVAD
GIDDPHFDAS NVGEYLQAAE VNAMLDDPDA LFIDMRNHYE YEVGHFENAL EIPADTFREQ
LPKAVEMMQA HKDKKIVMYC TGGIRCEKAS AWMKHNGFNK VWHIEGGIIE YARKAREQGL
PVRFIGKNFV FDERMGERIS DEIIAHCHQC GAPCDSHTNC KNDGCHLLFI QCPVCAEKYK
GCCSEICCEE SALPPEEQRR RRAGRENGNK IFNKSRGRLN TTLGIPDPTE
