ID A0A420EC48_9SPHN Unreviewed; 322 AA.
AC A0A420EC48;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 15.
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=D6851_14880 {ECO:0000313|EMBL:RKF18258.1};
OS Altericroceibacterium spongiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altericroceibacterium.
OX NCBI_TaxID=2320269 {ECO:0000313|EMBL:RKF18258.1, ECO:0000313|Proteomes:UP000284395};
RN [1] {ECO:0000313|EMBL:RKF18258.1, ECO:0000313|Proteomes:UP000284395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-Y73 {ECO:0000313|EMBL:RKF18258.1,
RC ECO:0000313|Proteomes:UP000284395};
RA Zhuang L., Luo L.;
RT "Altererythrobacter spongiae sp. nov., isolated from a marine sponge.";
RL Submitted (SEP-2018) 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:RKF18258.1}.
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DR EMBL; RAPF01000010; RKF18258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420EC48; -.
DR OrthoDB; 9778326at2; -.
DR Proteomes; UP000284395; 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; 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:UP000284395};
KW Transferase {ECO:0000313|EMBL:RKF18258.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 127..225
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 283..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 36083 MW; AC88109BFF51FA2A CRC64;
MTKANLPICV AALYQFTPFD DHAALQQPLL DACLAQGVKG TLLLAHEGIN GTIAGSDAGI
EATLDYIRTL PGCAAIEVKI SRALEMPFYR MKVRLKKEIV TMGEPDIDPV EGVGAYVAPD
EWNALIEDPD TIVIDTRNDY EVAIGTFKGA IDPKTKSFRE FPEWFQQHRA EFAKDGKQPK
IAMFCTGGIR CEKATAYVKA QGLDDVYHLK GGILAYLEQV PEERSTWEGD CFVFDERVSV
KHGLHLGDYA LCRACRMPLT REECESDLYE EGVSCPYCHE ERTDEQRRRY AERQRQTELA
EQRGMTHIAA AADQELSHKA DD
//
