ID A0A0M0G2C3_9BACI Unreviewed; 321 AA.
AC A0A0M0G2C3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AF331_15715 {ECO:0000313|EMBL:KON83626.1};
OS Rossellomorea marisflavi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189381 {ECO:0000313|EMBL:KON83626.1, ECO:0000313|Proteomes:UP000037405};
RN [1] {ECO:0000313|Proteomes:UP000037405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14235 jcm11544.";
RL Submitted (JUL-2015) 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:KON83626.1}.
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DR EMBL; LGUE01000005; KON83626.1; -; Genomic_DNA.
DR RefSeq; WP_053429049.1; NZ_LGUE01000005.1.
DR AlphaFoldDB; A0A0M0G2C3; -.
DR STRING; 189381.GCA_900166615_02001; -.
DR GeneID; 42293382; -.
DR PATRIC; fig|189381.12.peg.4125; -.
DR OrthoDB; 9778326at2; -.
DR Proteomes; UP000037405; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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: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; 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:UP000037405};
KW Transferase {ECO:0000313|EMBL:KON83626.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 124..218
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 321 AA; 37748 MW; 2CBA02EC9BC0D10E CRC64;
MNDYRVLLYY NYTQVEDAEA YAPQHKAKCE EIGLLGRILI SEEGINGTCS GTVEQTDAYM
EYMKNDPRFK DTVFKIEETD GHAFKKLKVK YRKELVTLRL EDDVDPNKLT GQYLEPKEFY
EQIQREDTIV LDARNDYEYD LGHFRGAIRP DIRNFRDLPQ WIRDNKEKFM DKKIITYCTG
GIRCEKFSGW LLKEGFEDVA QLHGGIVTYG QDPEVQGDLW DGQLYVFDER ISVPVNRKEH
VVIARDFYDG EPCERYVNCA YPPCNQKIIC SEENEHKYMR SCSHECRTHP ENRYVQEYGM
TEEEVAERLA VIEREKETAA I
//
