ID   TRUA_MYCGA              Reviewed;         263 AA.
AC   Q7NAQ9;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 88.
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=MYCGA5760;
GN   ORFNames=MGA_1331d;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(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}.
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DR   EMBL; AE015450; AAP56926.2; -; Genomic_DNA.
DR   RefSeq; WP_011113833.1; NC_004829.2.
DR   AlphaFoldDB; Q7NAQ9; -.
DR   SMR; Q7NAQ9; -.
DR   KEGG; mga:MGA_1331d; -.
DR   PATRIC; fig|233150.7.peg.648; -.
DR   HOGENOM; CLU_014673_0_1_14; -.
DR   OrthoDB; 1075262at2; -.
DR   Proteomes; UP000001418; 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..263
FT                   /note="tRNA pseudouridine synthase A"
FT                   /id="PRO_0000057408"
FT   ACT_SITE        73
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ   SEQUENCE   263 AA;  31104 MW;  89CF7E5A920F1280 CRC64;
     MVYLVHQNEW RSVWVKTLAK LNKNVLINIS YHGTKFHGYA VQNDYETVQS KLQDALAWIY
     ESKIYVNASG RTDKGVHAIN QYISFYIDDR ISLEKLREIL NRYGQNKWYI KWIKEVDRNF
     HARFSAKAKT YLYLIDYCAN NPLFYDHAWI VNFQLDFNLI EKAIPILEGT HNFWSFSTAD
     KDKGLRTIHK IDLKQEDNKV YIYITGDGFL RSMVRMIVGA LYNIGIKKYD LNHLKWLLDN
     PKKGRAITKA PASGLYLYEV YYE