TRUA_ECO57
ID TRUA_ECO57 Reviewed; 270 AA.
AC P65845; Q8XCR2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Z3580, ECs3202;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57447.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36625.1; -; Genomic_DNA.
DR PIR; B91029; B91029.
DR PIR; C85873; C85873.
DR RefSeq; NP_311229.1; NC_002695.1.
DR RefSeq; WP_001283590.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P65845; -.
DR SMR; P65845; -.
DR STRING; 155864.EDL933_3484; -.
DR EnsemblBacteria; AAG57447; AAG57447; Z3580.
DR EnsemblBacteria; BAB36625; BAB36625; ECs_3202.
DR GeneID; 66673799; -.
DR GeneID; 912282; -.
DR KEGG; ece:Z3580; -.
DR KEGG; ecs:ECs_3202; -.
DR PATRIC; fig|386585.9.peg.3342; -.
DR eggNOG; COG0101; Bacteria.
DR HOGENOM; CLU_014673_0_2_6; -.
DR OMA; FLYGMVR; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; tRNA processing.
FT CHAIN 1..270
FT /note="tRNA pseudouridine synthase A"
FT /id="PRO_0000057377"
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; 30385 MW; 9F1FD578B011D878 CRC64;
MSDQQQPPVY KIALGIEYDG SKYYGWQRQN EVRSVQEKLE KALSQVANEP ITVFCAGRTD
AGVHGTGQVV HFETTAQRKD AAWTLGVNAN LPGDIAVRWV KAVPDDFHAR FSATARRYRY
IIYNHRLRPA VLSKGVTHFY EPLDAERMHR AAQCLLGEND FTSFRAVQCQ SRTPWRNVMH
INVTRHGPYV VVDIKANAFV HHMVRNIVGS LMEVGAHNQP ESWIAELLAA KDRTLAAATA
KAEGLYLVAV DYPDRYDLPK PPMGPLFLAD
