ID Q05XX4_9SYNE Unreviewed; 315 AA.
AC Q05XX4;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 68.
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=RS9916_31352 {ECO:0000313|EMBL:EAU74096.1};
OS Synechococcus sp. RS9916.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=221359 {ECO:0000313|EMBL:EAU74096.1, ECO:0000313|Proteomes:UP000004972};
RN [1] {ECO:0000313|EMBL:EAU74096.1, ECO:0000313|Proteomes:UP000004972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS9916 {ECO:0000313|EMBL:EAU74096.1,
RC ECO:0000313|Proteomes:UP000004972};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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:EAU74096.1}.
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DR EMBL; AAUA01000001; EAU74096.1; -; Genomic_DNA.
DR RefSeq; WP_007098202.1; NZ_DS022299.1.
DR AlphaFoldDB; Q05XX4; -.
DR STRING; 221359.RS9916_31352; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_0_0_3; -.
DR OrthoDB; 9778326at2; -.
DR Proteomes; UP000004972; 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; IPR020936; TrhO.
DR InterPro; IPR040503; TRHO_N.
DR PANTHER; PTHR43268:SF3; RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 7-RELATED; 1.
DR PANTHER; PTHR43268; THIOSULFATE SULFURTRANSFERASE/RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF00581; Rhodanese; 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:UP000004972};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 135..233
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 315 AA; 35338 MW; 7FFF3CDEEFBA2810 CRC64;
MSTAAPNPLL VAAFYAFTPL TEDTRADLLE VLPGLAETGD VRGSVLVALE GVNGTISGPA
PAVEAVLDLL RQQLTLGDEH FARLEVKRSW CERQAFRRFK ARRKKEIVTM GCPDVSPIRT
VGTYVEPEQW NALIDDPDTL VIDTRNSYEV AIGSFEGALD PGTESFREFP AWAERTLRPR
VERDAPKRIA MFCTGGIRCE KATSYLQQQG FGEVHHLRGG ILKYLEEVPE ADSRWSGECF
VFDQRVALNH RLEQGVHRLC HACGLPLTPE QRALESYIRG VQCLHCIDRF TDADRQRFAE
RQRQLDQAKA SVESP
//
