ID TRUA_BORBU Reviewed; 246 AA. AC P70830; O51045; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 02-SEP-2026, entry version 135. 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}; GN OrderedLocusNames=BB_0012; OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OS (Borrelia burgdorferi). OC Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales; OC Borreliaceae; Borreliella. OX NCBI_TaxID=224326; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=HB19; RA Boursaux-Eude C., Margarita D., Belfaiza J., Old I.G., Saint-Girons I.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."; RL Nature 390:580-586(1997). 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; Y09141; CAA70351.1; -; Genomic_DNA. DR EMBL; AJ224474; CAA11967.1; -; Genomic_DNA. DR EMBL; AE000783; AAC66394.1; -; Genomic_DNA. DR PIR; D70101; D70101. DR RefSeq; WP_010889660.1; NC_001318.1. DR AlphaFoldDB; P70830; -. DR SMR; P70830; -. DR STRING; 224326.BB_0012; -. DR PaxDb; 224326-BB_0012; -. DR EnsemblBacteria; AAC66394; AAC66394; BB_0012. DR GeneID; 46847253; -. DR KEGG; bbu:BB_0012; -. DR PATRIC; fig|224326.49.peg.410; -. DR HOGENOM; CLU_014673_0_1_12; -. DR OrthoDB; 9811823at2; -. DR Proteomes; UP000001807; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0160147; F:tRNA pseudouridine(38-40) synthase activity; IEA:UniProtKB-EC. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule. DR CDD; cd02570; PseudoU_synth_EcTruA; 1. DR FunFam; 3.30.70.580:FF:000001; tRNA pseudouridine synthase A; 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 NCBIfam; TIGR00071; hisT_truA; 1. DR PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1. DR PANTHER; PTHR11142:SF0; TRNA PSEUDOURIDINE SYNTHASE-LIKE 1; 1. DR Pfam; PF01416; PseudoU_synth_1; 2. 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..246 FT /note="tRNA pseudouridine synthase A" FT /id="PRO_0000057341" FT ACT_SITE 52 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171" FT BINDING 111 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171" FT CONFLICT 59 FT /note="K -> R (in Ref. 1; CAA70351/CAA11967)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="I -> M (in Ref. 1; CAA70351/CAA11967)" FT /evidence="ECO:0000305" SQ SEQUENCE 246 AA; 28657 MW; B1F408385FF171A7 CRC64; MKKILAEIAY DGSIYHGFQI QPTKPTVQGE IEKALMKINK KKVKIHSSGR TDKGVHAKKQ IITFDIKINI QLNNLKKALN AILLKNSIKI LKLRYVKNSF HPRFSAQKRK YSYCILNSDN YYPWEGYQAH YVNKKLSISN LNQMAKTLIG KHDFTTFSCI KDKSKSKFRH IYFAKFKKRG KYIIFEIIGS SFLWKMVRSI IGTMLDIEIK NESISTFETI LKSKNRNLAR TTAPANALFL ERVYYE //