TRHO_FRATF
ID TRHO_FRATF Reviewed; 332 AA.
AC A7NCF1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
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}; OrderedLocusNames=FTA_1178;
OS Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=458234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FTNF002-00 / FTA;
RX PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA Lion C., Dempsey M.P.;
RT "Complete genome sequence of Francisella tularensis subspecies holarctica
RT FTNF002-00.";
RL PLoS ONE 4:E7041-E7041(2009).
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; CP000803; ABU61654.2; -; Genomic_DNA.
DR AlphaFoldDB; A7NCF1; -.
DR SMR; A7NCF1; -.
DR PRIDE; A7NCF1; -.
DR KEGG; fta:FTA_1178; -.
DR HOGENOM; CLU_038878_0_0_6; -.
DR OMA; CDTHTNC; -.
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; tRNA processing.
FT CHAIN 1..332
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_1000081190"
FT DOMAIN 127..221
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT REGION 308..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 332 AA; 38226 MW; 6F7B9663959B43DC CRC64;
MGIYMSQIVV CAMYKFVTLE DFEAMRQPLL DTMIKNNVKG TLLLANEGIN GTVAGTRESI
DNLLAYLKAD PRLVDIDYKE SYHQEMPFYR SKVKLKKEIV TLGIDEIDPN KICGKYVEPK
DWNDLISDPE TVLIDTRNEY EIEIGTFKNA INPHTENFRE FPQYVDENLD PKKHKKVAMF
CTGGIRCEKS TALLKAKGFD EVYHLKGGIL KYLEEVPKEK SMWQGECFVF DSRVAVNHDL
EKGNYDQCFA CRMPITEDDK KRPEYVKGIS CHHCYDKVTE KQKARFAERE KQSQLAAEKG
FSHVGDEAKK LAQLNKQKKQ QAKEAARKKA QQ