TRHO_ANAMM
ID TRHO_ANAMM Reviewed; 277 AA.
AC Q5PBC6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=AM315;
OS Anaplasma marginale (strain St. Maries).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=234826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St. Maries;
RX PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT is skewed to two superfamilies of outer membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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; CP000030; AAV86403.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5PBC6; -.
DR SMR; Q5PBC6; -.
DR PRIDE; Q5PBC6; -.
DR KEGG; ama:AM315; -.
DR HOGENOM; CLU_038878_0_1_5; -.
DR OMA; CDTHTNC; -.
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; tRNA processing.
FT CHAIN 1..277
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_0000161435"
FT DOMAIN 126..221
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT ACT_SITE 181
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 277 AA; 31852 MW; 34DD4B41C33A7EB5 CRC64;
MLFRAMGYVI AAFYRFVHLH NYYDMKPVIL EFCLSRGIKG TVILAEQGIN ATIAGSRQSI
GEFFSFLDSD DRLRGMKYHE SHSDREPFAK MKVRLKREVV RLGIDGFDCS LRGEYIDPRD
WDEFVSSPDV HVIDTRNDYE VRLGRFKGAI DPGTSSFREF PEWARNWALD KERDTCVAMY
CTGGIRCEKS TAFMRSLGFR NVYHLRGGIL NYLETMRGDD SLWEGECFVF DDRIAVDRNV
SPSEDIKCIK CAGEVDASDL RSVSKGNIMC WDCRLQA