ID B1VAF6_PHYAS Unreviewed; 306 AA.
AC B1VAF6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=tRNA uridine(34) hydroxylase {ECO:0000256|HAMAP-Rule:MF_00469};
DE EC=1.14.-.- {ECO:0000256|HAMAP-Rule:MF_00469};
DE AltName: Full=tRNA hydroxylation protein O {ECO:0000256|HAMAP-Rule:MF_00469};
GN Name=trhO {ECO:0000256|HAMAP-Rule:MF_00469};
GN OrderedLocusNames=PA0595 {ECO:0000313|EMBL:CAM11929.1};
OS Phytoplasma australiense.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrXII (Stolbur group).
OX NCBI_TaxID=59748 {ECO:0000313|EMBL:CAM11929.1, ECO:0000313|Proteomes:UP000008323};
RN [1] {ECO:0000313|EMBL:CAM11929.1, ECO:0000313|Proteomes:UP000008323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18359806; DOI=10.1128/JB.01301-07;
RA Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT and AY-WB.";
RL J. Bacteriol. 190:3979-3991(2008).
CC -!- FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U)
CC modification at position 34 in tRNAs. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00469};
CC -!- SIMILARITY: Belongs to the TrhO family. {ECO:0000256|HAMAP-
CC Rule:MF_00469}.
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DR EMBL; AM422018; CAM11929.1; -; Genomic_DNA.
DR AlphaFoldDB; B1VAF6; -.
DR STRING; 59748.PA0595; -.
DR KEGG; pal:PA0595; -.
DR eggNOG; COG1054; Bacteria.
DR Proteomes; UP000008323; 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 CDD; cd01518; RHOD_YceA; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 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:SF3; RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 7-RELATED; 1.
DR PANTHER; PTHR43268; THIOSULFATE SULFURTRANSFERASE/RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 2; 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; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00469};
KW Reference proteome {ECO:0000313|Proteomes:UP000008323};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 127..221
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 306 AA; 36125 MW; ADA4F8E24644FC10 CRC64;
MTPTKEYQVI LYYQYTKIDD VQLFRDNHFK YCQSLELQGR VIVSQEGING TLSGTKSNLQ
TYMQHLKKDH RFSDIVFKID QATKHLFPRL SVKVKKEIVN FNFNQELDMD KNKGTYLTPE
SFYHAMQQKD TLILDARNDY EYDVGHFRNA LNPKIKHFRD LPEWVEKNVS LLQNQKILTY
CTGGVRCEKF SSFLKQKGIQ EVYQLEGGVI SYMQNPQTQG VLWDGQMYVF DQRITIPVNQ
KEHVIVGKDY FDQTPCERYI NCSNPECNKQ ILCNEENEHK YLGACSKKCR LHPSNRYLLK
RNNQQL
//
