TRUA_BIFA0
ID TRUA_BIFA0 Reviewed; 298 AA.
AC B8DW40;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=BLA_0389;
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=442563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011;
RX PubMed=19011029; DOI=10.1128/jb.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001213; ACL28691.1; -; Genomic_DNA.
DR RefSeq; WP_012619707.1; NC_011835.1.
DR AlphaFoldDB; B8DW40; -.
DR SMR; B8DW40; -.
DR STRING; 442563.BLA_0389; -.
DR EnsemblBacteria; ACL28691; ACL28691; BLA_0389.
DR GeneID; 66532772; -.
DR KEGG; bla:BLA_0389; -.
DR HOGENOM; CLU_014673_0_2_11; -.
DR OMA; FLYGMVR; -.
DR Proteomes; UP000002456; 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; 3.30.70.580; -; 1.
DR Gene3D; 3.30.70.660; -; 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; PTHR11142; 1.
DR Pfam; PF01416; PseudoU_synth_1; 1.
DR PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00071; hisT_truA; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; tRNA processing.
FT CHAIN 1..298
FT /note="tRNA pseudouridine synthase A"
FT /id="PRO_1000194529"
FT ACT_SITE 56
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ SEQUENCE 298 AA; 32607 MW; D0D17A98048BFF60 CRC64;
MTRLRIDLAY NGAAFHGWAA QPGCRTVQGT VEEALRRITR MPDAGSLRLT VAGRTDAGVH
ATHQVCHVDV PDQTLGQCVG HMNLTPVQAL QTRLSRMMPD DIAIHGISVA PAGFDARFSA
LERTYVYRIA DARVPWDPRL KDFAWRTDRE LDIAQMNAAA ALTLGLHDFG SFAIANPGGT
TIREVKTAYW QRVPTRPLLG PGMGERYHTP AVESGLLCFT IVADAFARNM VRSLVGACVQ
VGMGKRDVDW FAGKMRVPLR EGSTGPIAPQ GLTLEHIAYP ADDELAARAE RIRAKRTL
