ID A0A147EM58_9MICO Unreviewed; 312 AA.
AC A0A147EM58;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tRNA uridine(34) hydroxylase {ECO:0000256|HAMAP-Rule:MF_00469};
DE EC=1.14.-.- {ECO:0000256|HAMAP-Rule:MF_00469};
DE AltName: Full=tRNA hydroxylation protein O {ECO:0000256|HAMAP-Rule:MF_00469};
GN Name=trhO {ECO:0000256|HAMAP-Rule:MF_00469};
GN ORFNames=NS354_09045 {ECO:0000313|EMBL:KTR85501.1};
OS Leucobacter chromiiresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR85501.1, ECO:0000313|Proteomes:UP000070810};
RN [1] {ECO:0000313|EMBL:KTR85501.1, ECO:0000313|Proteomes:UP000070810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS354 {ECO:0000313|EMBL:KTR85501.1,
RC ECO:0000313|Proteomes:UP000070810};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
CC -!- FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U)
CC modification at position 34 in tRNAs. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00469};
CC -!- SIMILARITY: Belongs to the TrhO family. {ECO:0000256|HAMAP-
CC Rule:MF_00469}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTR85501.1}.
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DR EMBL; LDRK01000056; KTR85501.1; -; Genomic_DNA.
DR RefSeq; WP_058594196.1; NZ_LDRK01000056.1.
DR AlphaFoldDB; A0A147EM58; -.
DR PATRIC; fig|1079994.3.peg.2021; -.
DR OrthoDB; 9778326at2; -.
DR Proteomes; UP000070810; Unassembled WGS sequence.
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 CDD; cd01518; RHOD_YceA; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 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; THIOSULFATE SULFURTRANSFERASE/RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR43268:SF6; THIOSULFATE SULFURTRANSFERASE_RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 2; 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; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00469};
KW Reference proteome {ECO:0000313|Proteomes:UP000070810};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 151..246
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 312 AA; 33881 MW; B8AB27F018F97AD4 CRC64;
MSEPKILLYY VFAPVADPEA VRLWQRELCE SLGLRGRIIV SPHGINGTVG GELDACKQYL
RRTREYPPFA ALEPKWSEGT ALVDAPEERL HGVERGARWQ RITDFPRLSV KVRDELVAFG
IPNETRVDSD GVVGGGVHLS PQEVNDLVAE RGDEVVFFDG RNAWEAEIGR FAGAVVPSTR
TTHDFIAQID AGDFDDLKGR PVVTYCTGGI RCEILSAAMR TRGFDEVYQI DGGIVKYGEA
FGNDGLWEGS LAVFDGREAL DFAPGAAVIG RCRVCGAPSN AVSNCSDPAC THRFVVCDAH
AGSPCEEHAQ AA
//
