ID TRUA_TROWT Reviewed; 267 AA.
AC Q83G11;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=tRNA pseudouridine synthase A {ECO:0000255|HAMAP-Rule:MF_00171};
DE EC=5.4.99.12 {ECO:0000255|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000255|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA pseudouridylate synthase I {ECO:0000255|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA-uridine isomerase I {ECO:0000255|HAMAP-Rule:MF_00171};
GN Name=truA {ECO:0000255|HAMAP-Rule:MF_00171}; OrderedLocusNames=TWT_526;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Tropherymataceae;
OC Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
CC -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the
CC anticodon stem and loop of transfer RNAs. {ECO:0000255|HAMAP-
CC Rule:MF_00171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA;
CC Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00171};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00171}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000255|HAMAP-Rule:MF_00171}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO44623.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014184; AAO44623.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q83G11; -.
DR SMR; Q83G11; -.
DR STRING; 203267.TWT_526; -.
DR KEGG; twh:TWT_526; -.
DR eggNOG; COG0101; Bacteria.
DR HOGENOM; CLU_014673_0_2_11; -.
DR OrthoDB; 9811823at2; -.
DR Proteomes; UP000002200; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd02570; PseudoU_synth_EcTruA; 1.
DR Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR HAMAP; MF_00171; TruA; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11142:SF0; TRNA PSEUDOURIDINE SYNTHASE-LIKE 1; 1.
DR Pfam; PF01416; PseudoU_synth_1; 1.
DR PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; tRNA processing.
FT CHAIN 1..267
FT /note="tRNA pseudouridine synthase A"
FT /id="PRO_0000057481"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ SEQUENCE 267 AA; 30576 MW; E5ACF841AF7A0104 CRC64;
MNKTRYRLDV AYDGANFCGW APQPGLRTVG GLILDALRLI CSEPPDIVVA ARTDAGVHAL
QQVCHVDLIS SPDPVWLLHR LRSLLKSETD LHILSAVKAP VNFHARFSAI GRRYVYRVID
KRSSWYPQNR YFVYRVNAFL QDYRMRRAAS GLIGLKDFGA FCKPRRMGST VRHLRQFEVI
RQPDGQIHFF LESDAFCHSM VRNLVGSLIE VGRGALTLQD LFCYTKIAKR TPKIPTLPPH
ALTLIGIDYP QEHLFECQNR KTRQKRT
//
