TRHO_LACLA
ID TRHO_LACLA Reviewed; 319 AA.
AC Q9CG88; O34131;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=ymdE;
GN OrderedLocusNames=LL1217; ORFNames=L38177;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 2118;
RA Delorme C., Goupil-Feuillerat N., Godon J.-J., Ehrlich S.D., Renault P.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; U92974; AAB81912.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05315.1; -; Genomic_DNA.
DR PIR; A86777; A86777.
DR PIR; E47754; E47754.
DR RefSeq; NP_267373.1; NC_002662.1.
DR RefSeq; WP_003131122.1; NC_002662.1.
DR AlphaFoldDB; Q9CG88; -.
DR SMR; Q9CG88; -.
DR STRING; 272623.L38177; -.
DR PaxDb; Q9CG88; -.
DR EnsemblBacteria; AAK05315; AAK05315; L38177.
DR KEGG; lla:L38177; -.
DR PATRIC; fig|272623.7.peg.1314; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_1_0_9; -.
DR OMA; CDTHTNC; -.
DR Proteomes; UP000002196; 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 PANTHER; PTHR43268; PTHR43268; 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; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Reference proteome; tRNA processing.
FT CHAIN 1..319
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_0000161480"
FT DOMAIN 125..219
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT ACT_SITE 179
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT CONFLICT 204
FT /note="H -> L (in Ref. 1; AAB81912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 36850 MW; F987D509415F169A CRC64;
MTQDYRVLLY YQYVPIEDGE TFAQKHLADC KELGLKGRIL VADEGINGTV SGTIEQTNAY
MELMKNDPRF SSTIFKIDEA EQNAFKKMHV RYRPELVNLS LEDDVNPLEL TGAYLDPKEF
REAMLDENTV VIDARNDYEF DLGHFRGAIR PEIRSFRELP QWIRDNKEQF MEKRVLTYCT
GGIRCEKFSG WLVREGFKDV GQLHGGIATY GKDPEVQGDL WDGQMYVFDS RIAVPINQKE
HVIVGRDWFD GSPCERYINC GNPECNRQML ASEENEAKYL GACSHECRVH PNNRYIKAHQ
LSNQEVQERL ALLEKDLAS