TRHO_PHOLL
ID TRHO_PHOLL Reviewed; 352 AA.
AC Q7N5W3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=plu1816;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571865; CAE14109.1; -; Genomic_DNA.
DR RefSeq; WP_011146093.1; NC_005126.1.
DR AlphaFoldDB; Q7N5W3; -.
DR SMR; Q7N5W3; -.
DR STRING; 243265.plu1816; -.
DR EnsemblBacteria; CAE14109; CAE14109; plu1816.
DR GeneID; 24166822; -.
DR KEGG; plu:plu1816; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_1_1_6; -.
DR OMA; CDTHTNC; -.
DR OrthoDB; 684577at2; -.
DR BioCyc; PLUM243265:PLU_RS09075-MON; -.
DR Proteomes; UP000002514; 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 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..352
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_0000161492"
FT DOMAIN 146..240
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT REGION 315..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 352 AA; 40418 MW; BA431404EE914A13 CRC64;
MPVLHNRISN KELKARMLAE TQPRTTISFY KYFNILNPLD FRNSLYQQFT DLSVFGRVYI
AKEGINAQIS LPTHNLEAFK ALLYSVDPAL DNLRLNIALD DDGKSFWVLR MKVRDRVVAD
GIDDETFDPS KTGEYLKAEQ VNQMLDNPDT LFVDMRNHYE YEVGHFENAI EVPSDTFREQ
LPMVAEMLQD NKDKNIVMYC TGGIRCEKAS AYMLHNGFKN VYHVEGGIIE YARKAREQGL
PVRFVGKNFV FDERMGERIS DDVIAHCHQC GVSCDSHTNC KNEGCHLLFI QCPECATKFE
GCCSEMCREE VRLPETEQRA RRAGRENGAK IFNKSRHRLQ DGLNSTSLQS VE