TRHO_ACIBY
ID TRHO_ACIBY Reviewed; 314 AA.
AC B0VEG5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=ABAYE0771;
OS Acinetobacter baumannii (strain AYE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509173;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYE;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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; CU459141; CAM85729.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VEG5; -.
DR SMR; B0VEG5; -.
DR EnsemblBacteria; CAM85729; CAM85729; ABAYE0771.
DR KEGG; aby:ABAYE0771; -.
DR HOGENOM; CLU_038878_0_0_6; -.
DR OMA; CDTHTNC; -.
DR Proteomes; UP000002446; 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; 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..314
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_1000200333"
FT DOMAIN 140..234
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT ACT_SITE 194
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 314 AA; 35528 MW; DBB6E10D7A4D0AC7 CRC64;
MEFSMNATVE QLAPVEQQAT AGWVVAALYQ FKEVQDPADL QQRLLDLVKT INLCGTLIVA
GEGINGTVAG DREAIDTIHQ FLLNEGFNAM EYKESHSSDK PFRKMKIKLK KEIVTLGVEV
KPRDLVGHYL DPKEWNELIA RDDVILIDTR NDYEYKAGTF KGAIDPKTET FREFPEYVKK
ELEQHKDKKI AMFCTGGIRC EKSTSLLLQE GFKEVYHLKG GILKYLEETP PDESLWEGEC
FVFDGRTAVT HGVEEGANIK CHACGWPLTP EESALPSYEH GVSCLYCIDK TTEKQKAGFR
MRQSQIAAAK RKRL