TRHO_LACLM
ID TRHO_LACLM Reviewed; 319 AA.
AC A2RKR4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=llmg_1287;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL97880.1; -; Genomic_DNA.
DR RefSeq; WP_011835164.1; NZ_WJVF01000013.1.
DR AlphaFoldDB; A2RKR4; -.
DR SMR; A2RKR4; -.
DR STRING; 416870.llmg_1287; -.
DR EnsemblBacteria; CAL97880; CAL97880; llmg_1287.
DR GeneID; 61109474; -.
DR KEGG; llm:llmg_1287; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_1_0_9; -.
DR OMA; CDTHTNC; -.
DR PhylomeDB; A2RKR4; -.
DR BioCyc; LLAC416870:LLMG_RS06525-MON; -.
DR Proteomes; UP000000364; 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; tRNA processing.
FT CHAIN 1..319
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_1000013744"
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"
SQ SEQUENCE 319 AA; 36740 MW; DC230758186A564F CRC64;
MTQDYRVLLY YQYVPIEDGE SFAQKHLSDC KALGLKGRIL VADEGINGTV SGTVEQTNAY
MSLMKNDSRF TSTIFKIDEA KQNAFKKMHV RYRPELVNLS LEDDVNPLEL TGAYLDPKEF
REAMLDENTV VIDARNDYEF DLGHFRGAIR PEIRSFRELP QWIRDNKEQF MEKRVLTYCT
GGIRCEKFSG WLVREGFKDV GQLHGGIATY GKDPEVQGDL WDGQMYVFDS RIAVPINQKE
HVIVGRDWFD GSPCERYINC GNPECNRQML ASKENEAKYL GACSHECRVH PDNRYIKAHQ
LSNQEVQERL ALLEKDLAS