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TRHO_PROMM
ID   TRHO_PROMM              Reviewed;         310 AA.
AC   Q7V6T9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=PMT_1055;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548175; CAE21230.1; -; Genomic_DNA.
DR   RefSeq; WP_011130427.1; NC_005071.1.
DR   AlphaFoldDB; Q7V6T9; -.
DR   SMR; Q7V6T9; -.
DR   STRING; 74547.PMT_1055; -.
DR   PRIDE; Q7V6T9; -.
DR   EnsemblBacteria; CAE21230; CAE21230; PMT_1055.
DR   KEGG; pmt:PMT_1055; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_0_0_3; -.
DR   OMA; CDTHTNC; -.
DR   OrthoDB; 684577at2; -.
DR   Proteomes; UP000001423; 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; IPR020936; TrhO.
DR   InterPro; IPR040503; TRHO_N.
DR   PANTHER; PTHR43268; PTHR43268; 1.
DR   Pfam; PF00581; Rhodanese; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..310
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000161495"
FT   DOMAIN          134..232
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        192
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   310 AA;  35122 MW;  664C10734BD283D8 CRC64;
     MNLQDDQTSA DLFQVATFYS FTAWTEVTIA CLLHDLLSLG DEHQLMGTVL LAEEGVNGTI
     CGSVDGVSAL LERLESDLIE GLFELKISWT PEQAFRRFKV RRKAEIVTMG LAGLNPSKTV
     GTYVDAHEWN DLIDDPDTLL IDTRNDYEVA IGEFKGAINP QTKCFRDFPA WVEQQLRSMV
     KAQTPARIAM YCTGGIRCEK ATSYLIEKGF TNVHHLRGGI LRYFEEVSQT ESRWQGECFV
     FDQRVALNHQ LSPGVHCLCH ACGMPLTPED QTMNSYLPGV QCRHCVDQFS DTDRIRFAER
     QRQMEHSSRK
 
 
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