TRUA_BUCA5
ID TRUA_BUCA5 Reviewed; 266 AA.
AC B8D8Z8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=BUAP5A_196;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=563178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5A;
RX PubMed=19150844; DOI=10.1126/science.1167140;
RA Moran N.A., McLaughlin H.J., Sorek R.;
RT "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT bacteria.";
RL Science 323:379-382(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; CP001161; ACL30569.1; -; Genomic_DNA.
DR RefSeq; WP_009874156.1; NC_011833.1.
DR AlphaFoldDB; B8D8Z8; -.
DR SMR; B8D8Z8; -.
DR KEGG; bap:BUAP5A_196; -.
DR HOGENOM; CLU_014673_0_2_6; -.
DR OMA; FLYGMVR; -.
DR OrthoDB; 1075262at2; -.
DR Proteomes; UP000006904; 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..266
FT /note="tRNA pseudouridine synthase A"
FT /id="PRO_1000194535"
FT ACT_SITE 57
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ SEQUENCE 266 AA; 30778 MW; A340825E9499D0A9 CRC64;
MVAKNVKTFA LGVEYDGSYY HGWQRQKIVP SIQEEIEKAL SIIANHKIDV VCAGRTDAGV
HSIGQVIHFK TTANRKKSSW SIGVNSYLSE NISVVWVKEV TENFHARYSA ITRSYRYIIY
NYSLRSAIFQ TKLNHIYRKL NVDKMHFEAQ FLLGEHDFTS FRALGCQSHS PWRNITKLNV
FRFHNWVVVD ITANSFLHHM VRNIVGSLIE VGISKKKEYW IKDLLEKKDR SHAGATAPAK
GLYLVYVEYP LHFNLPRSAY TSIFFK