TRHO_SALAR
ID TRHO_SALAR Reviewed; 350 AA.
AC A9MH08;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=SARI_01842;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX21727.1; -; Genomic_DNA.
DR RefSeq; WP_001144650.1; NC_010067.1.
DR AlphaFoldDB; A9MH08; -.
DR SMR; A9MH08; -.
DR STRING; 41514.SARI_01842; -.
DR EnsemblBacteria; ABX21727; ABX21727; SARI_01842.
DR KEGG; ses:SARI_01842; -.
DR HOGENOM; CLU_038878_1_1_6; -.
DR OMA; CDTHTNC; -.
DR OrthoDB; 684577at2; -.
DR Proteomes; UP000002084; 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_1000081194"
FT DOMAIN 146..240
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT REGION 318..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 350 AA; 39862 MW; 19DF1B500CC61B1E CRC64;
MPVLHNRISN DELKARMLAE SEPRTTISFY KYFTIVSPQQ TRDALYQMFT ALGIFGRVYL
AHEGINAQIS VPQSKVETFR QQLYAFDPAL DGLRLNIALE DDGKSFWVLR MKVRDRIVAD
GIDDPSFDAS NVGAYLKAAE VNAMLDDPDA IFIDMRNHYE YEVGHFENAL EIPADTFREQ
LPKAVEMLRE HADKKIVMYC TGGIRCEKAS AWMKHNGFNK VWHIEGGIIE YARRAREQGL
PVRFIGKNFV FDERMGERIS DEVIAHCHQC GALCDSHTNC KNAGCHLLFI QCPLCASKFN
GCCSEQCCEE LALPEDEQRR RRAGREKGNK IFNKSRGRLN SKLGIPDPTE
