TRHO_LEGPH
ID TRHO_LEGPH Reviewed; 254 AA.
AC Q5ZRP2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=lpg2838;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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; AE017354; AAU28886.1; -; Genomic_DNA.
DR RefSeq; WP_010948525.1; NC_002942.5.
DR RefSeq; YP_096833.1; NC_002942.5.
DR PDB; 4F67; X-ray; 1.79 A; A=1-254.
DR PDBsum; 4F67; -.
DR AlphaFoldDB; Q5ZRP2; -.
DR SMR; Q5ZRP2; -.
DR STRING; 272624.lpg2838; -.
DR PaxDb; Q5ZRP2; -.
DR DNASU; 3079754; -.
DR EnsemblBacteria; AAU28886; AAU28886; lpg2838.
DR GeneID; 66492009; -.
DR KEGG; lpn:lpg2838; -.
DR PATRIC; fig|272624.6.peg.3023; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_0_1_6; -.
DR OMA; CDTHTNC; -.
DR Proteomes; UP000000609; 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 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome; tRNA processing.
FT CHAIN 1..254
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_0000161484"
FT DOMAIN 123..217
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT ACT_SITE 177
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:4F67"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:4F67"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:4F67"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4F67"
SQ SEQUENCE 254 AA; 29904 MW; D71F02C16B6FEAC4 CRC64;
MKDIIIASFY KFIPLNDFES LREPILTKMH EIGIKGTIIL AHEGVNGGFA GNREQMNVFY
DYLRSDSRFA DLHFKETYDN KNPFDKAKVK LRKEIVTMGV QKVDPSYNAG TYLSPEEWHQ
FIQDPNVILL DTRNDYEYEL GTFKNAINPD IENFREFPDY VQRNLIDKKD KKIAMFCTGG
IRCEKTTAYM KELGFEHVYQ LHDGILNYLE SIPESESLWE GKCFVFDDRV AVDQKLDRVY
PQLPQDYKYE REQK
