ID   TRUA_ECOHS              Reviewed;         270 AA.
AC   A8A2I7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=EcHS_A2469;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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}.
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DR   EMBL; CP000802; ABV06741.1; -; Genomic_DNA.
DR   RefSeq; WP_001283585.1; NC_009800.1.
DR   AlphaFoldDB; A8A2I7; -.
DR   SMR; A8A2I7; -.
DR   KEGG; ecx:EcHS_A2469; -.
DR   HOGENOM; CLU_014673_0_2_6; -.
DR   OMA; FLYGMVR; -.
DR   Proteomes; UP000001123; 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; 2.
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; tRNA processing.
FT   CHAIN           1..270
FT                   /note="tRNA pseudouridine synthase A"
FT                   /id="PRO_1000058305"
FT   REGION          107..111
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   REGION          168..172
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   ACT_SITE        60
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   SITE            58
FT                   /note="Interaction with tRNA; Important for base-flipping"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   SITE            78
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   SITE            110
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   SITE            126
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   SITE            139
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ   SEQUENCE   270 AA;  30370 MW;  853D1D8373331088 CRC64;
     MSDQQQPPVY KIALGIEYDG SKYYGWQRQN EVRSVQEKLE KALSQVANEP ITVFCAGRTD
     AGVHGTGQVV HFETTALRKD AAWTLGVNAN LPGDIAVRWV KAVPDDFHAR FSATARRYRY
     IIYNHRLRPA VLSKGVTHFY EPLDAERMHR AAQCLLGEND FTSFRAVQCQ SRTPWRNVMH
     INVTRHGPYV VVDIKANAFV HHMVRNIVGS LMEVGAHNQP ESWIAELLAA KDRTLAAATA
     KAEGLYLVAV DYPDRYDLPK PPMGPLFLAD