TRHO_PSEMY
ID TRHO_PSEMY Reviewed; 312 AA.
AC A4XSZ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, 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=Pmen_1693;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000680; ABP84457.1; -; Genomic_DNA.
DR RefSeq; WP_003245074.1; NC_009439.1.
DR AlphaFoldDB; A4XSZ1; -.
DR SMR; A4XSZ1; -.
DR STRING; 399739.Pmen_1693; -.
DR EnsemblBacteria; ABP84457; ABP84457; Pmen_1693.
DR KEGG; pmy:Pmen_1693; -.
DR PATRIC; fig|399739.8.peg.1716; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_0_0_6; -.
DR OMA; CDTHTNC; -.
DR OrthoDB; 684577at2; -.
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..312
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_1000060371"
FT DOMAIN 124..218
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT REGION 279..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 312 AA; 35528 MW; 4A696ABF108B0DEB CRC64;
MTDKIVVAAL YKFVSLPDYQ ALREPLLQTL LDNGIKGTLL LAEEGINGTV SGSRAAIDAL
LAWFRQDARL ADIDHKESYC DEQPFYRTKV KLKKEIVTLG VPGVDPNQRV GTYVEPQDWN
ALISDPEVLL IDTRNDYEVA IGTFEGAIDP KTKSFREFPE YVKAHFDPSK HKKVAMFCTG
GIRCEKASSY MLGEGFEEVY HLKGGILKYL EEVPQEQTKW RGDCFVFDNR VTVRHDLSEG
DYDQCHACRN PISVEDRQSE YYSPGVSCPH CWDSLPEKTR ESARERQKQI ELARARNQPH
PIGRDPRQLN EA