TRHO_ECOLI
ID TRHO_ECOLI Reviewed; 350 AA.
AC P24188; P75924;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=tRNA uridine(34) hydroxylase {ECO:0000305};
DE EC=1.14.-.- {ECO:0000269|PubMed:31253794};
DE AltName: Full=ORF39.9;
DE AltName: Full=tRNA hydroxylation protein O {ECO:0000303|PubMed:31253794};
GN Name=trhO {ECO:0000303|PubMed:31253794}; Synonyms=yceA;
GN OrderedLocusNames=b1055, JW1042;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1840644; DOI=10.1111/j.1365-2958.1991.tb02159.x;
RA Karow M.L., Georgopoulos C.;
RT "Sequencing, mutational analysis, and transcriptional regulation of the
RT Escherichia coli htrB gene.";
RL Mol. Microbiol. 5:2285-2292(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LYS-112; ARG-114; CYS-200; THR-201; GLY-202; GLY-203; ARG-205 AND CYS-206.
RX PubMed=31253794; DOI=10.1038/s41467-019-10750-8;
RA Sakai Y., Kimura S., Suzuki T.;
RT "Dual pathways of tRNA hydroxylation ensure efficient translation by
RT expanding decoding capability.";
RL Nat. Commun. 10:2858-2858(2019).
CC -!- FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U)
CC modification at position 34 in tRNAs, the first step in 5-
CC carboxymethoxyuridine (cmo5U) biosynthesis (PubMed:31253794). May be
CC part of an alternate pathway, which is able to bypass cmo5U biogenesis
CC in a subset of tRNAs under aerobic conditions (PubMed:31253794).
CC {ECO:0000269|PubMed:31253794}.
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:0000269|PubMed:31253794};
CC -!- INTERACTION:
CC P24188; P0A7K2: rplL; NbExp=3; IntAct=EBI-560455, EBI-543702;
CC -!- INDUCTION: Is expressed at all temperatures, but accumulation of yceA
CC transcripts decline with raising temperature. Thus, its expression is
CC repressed by heat shock. {ECO:0000269|PubMed:1840644}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant displays only slight reduction of
CC 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs
CC (PubMed:31253794). Cells lacking both trhP and trhO show complete
CC absence of 5-carboxymethoxyuridine (cmo5U) modification in tRNAs; cells
CC display a temperature-sensitive phenotype and decode codons ending in G
CC (GCG and UCG) less efficiently than the wild-type strain
CC (PubMed:31253794). {ECO:0000269|PubMed:31253794}.
CC -!- SIMILARITY: Belongs to the TrhO family. {ECO:0000255|HAMAP-
CC Rule:MF_00469}.
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DR EMBL; X61000; CAA43318.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74139.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35853.1; -; Genomic_DNA.
DR PIR; D64848; D64848.
DR RefSeq; NP_415573.1; NC_000913.3.
DR RefSeq; WP_001144615.1; NZ_SSZK01000058.1.
DR AlphaFoldDB; P24188; -.
DR SMR; P24188; -.
DR BioGRID; 4262843; 125.
DR DIP; DIP-11521N; -.
DR IntAct; P24188; 7.
DR STRING; 511145.b1055; -.
DR PaxDb; P24188; -.
DR PRIDE; P24188; -.
DR EnsemblBacteria; AAC74139; AAC74139; b1055.
DR EnsemblBacteria; BAA35853; BAA35853; BAA35853.
DR GeneID; 945601; -.
DR KEGG; ecj:JW1042; -.
DR KEGG; eco:b1055; -.
DR PATRIC; fig|1411691.4.peg.1214; -.
DR EchoBASE; EB1106; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_1_1_6; -.
DR InParanoid; P24188; -.
DR OMA; CDTHTNC; -.
DR PhylomeDB; P24188; -.
DR BioCyc; EcoCyc:EG11116-MON; -.
DR BioCyc; MetaCyc:EG11116-MON; -.
DR PRO; PR:P24188; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:EcoCyc.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Oxidoreductase; Reference proteome; tRNA processing.
FT CHAIN 1..350
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_0000161470"
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"
FT MUTAGEN 112
FT /note="K->A: Reduced 5-carboxymethoxyuridine formation."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 114
FT /note="R->A: Reduced 5-carboxymethoxyuridine formation."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 200
FT /note="C->A: Reduced 5-carboxymethoxyuridine formation."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 201
FT /note="T->A: Reduced 5-carboxymethoxyuridine formation."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 202
FT /note="G->A: Does not affect 5-carboxymethoxyuridine
FT formation."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 203
FT /note="G->A: Reduced 5-carboxymethoxyuridine formation."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 205
FT /note="R->A: Reduced 5-carboxymethoxyuridine formation."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 206
FT /note="C->A: Does not affect 5-carboxymethoxyuridine
FT formation."
FT /evidence="ECO:0000269|PubMed:31253794"
FT CONFLICT 82..83
FT /note="QL -> HV (in Ref. 1; CAA43318)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="A -> R (in Ref. 1; CAA43318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 39781 MW; 61AB5F317B0C221B 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 TTLCIPDPTE
