TRHO_LISW6
ID TRHO_LISW6 Reviewed; 319 AA.
AC A0AII6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=lwe1400;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK20818.1; -; Genomic_DNA.
DR RefSeq; WP_011702196.1; NC_008555.1.
DR AlphaFoldDB; A0AII6; -.
DR SMR; A0AII6; -.
DR STRING; 386043.lwe1400; -.
DR EnsemblBacteria; CAK20818; CAK20818; lwe1400.
DR GeneID; 61189276; -.
DR KEGG; lwe:lwe1400; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_1_0_9; -.
DR OMA; CDTHTNC; -.
DR OrthoDB; 684577at2; -.
DR Proteomes; UP000000779; 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_1000013749"
FT DOMAIN 124..218
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT ACT_SITE 178
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 319 AA; 36434 MW; AAFC38653CEFF332 CRC64;
MSDYQVLLYY KYTTIDDPET FAKEHLAACK EMELKGRILV ASEGINGTVS GTVEATNKYM
DYMANDARFA DMVFKIDAAD SHAFKKMHVR PRAEIVSLSL EEDVNPLEVT GTYLEPTEFR
EALLDEDTVI LDARNDYEFD IGHFRGAVRP DIQNFRELPG WIEENRDQLA DKKIVTYCTG
GIRCEKFSGW LKTAGFEDVS QLHGGIATYG KNEETKGELW DGQMYVFDER IAVPINQVNP
TIVGKDYFDG TPCERYINCA NPYCNKQILA SIENEEKYLR SCSHECRVHP ANLYTKELSK
EEFTERLQAI SETSPEMVQ