TRHO_PECCP
ID TRHO_PECCP Reviewed; 355 AA.
AC C6DKU9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=PC1_2519;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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; CP001657; ACT13550.1; -; Genomic_DNA.
DR RefSeq; WP_015840725.1; NC_012917.1.
DR AlphaFoldDB; C6DKU9; -.
DR SMR; C6DKU9; -.
DR STRING; 561230.PC1_2519; -.
DR EnsemblBacteria; ACT13550; ACT13550; PC1_2519.
DR KEGG; pct:PC1_2519; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_1_1_6; -.
DR OMA; CDTHTNC; -.
DR OrthoDB; 684577at2; -.
DR Proteomes; UP000002736; 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; tRNA processing.
FT CHAIN 1..355
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_1000206338"
FT DOMAIN 146..240
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT ACT_SITE 200
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 355 AA; 40327 MW; C746076308347B5E CRC64;
MPVLHNRISN EELKARMLAE TEPRTTVSFY KYFTIDDPKA FRDRLYIQLE QCKVLGRIYI
ATEGINAQIS VPNNQFDAFK AVLFSAHPAL DQIRLNIALE DDGKSFWVLR MKVRERIVAD
GIDDPTFNPA NVGQYLKADQ VNAMADDPDT VFVDMRNHYE YEVGHFENAL EVPSDTFREQ
LPMAVEMLDE ARDKNIVMYC TGGIRCEKAS AYMLHHGFKN VYHVEGGIIE YARQAKAQGL
PLKFIGKNFV FDERMGERIS DDVIAHCHQC GASCDSHTNC RNEGCHLLFI QCPTCAAKYE
GCCSTQCLDE MKLPLEEQRA IRSGRENGMK IFNKSKGLLQ STLHIPAPEV KDKAE