ID TRUA_BUCBP Reviewed; 264 AA.
AC P59508;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
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=bbp_185;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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; AE016826; AAO26917.1; -; Genomic_DNA.
DR RefSeq; WP_011091318.1; NC_004545.1.
DR AlphaFoldDB; P59508; -.
DR SMR; P59508; -.
DR STRING; 224915.bbp_185; -.
DR KEGG; bab:bbp_185; -.
DR eggNOG; COG0101; Bacteria.
DR HOGENOM; CLU_014673_0_2_6; -.
DR OrthoDB; 9811823at2; -.
DR Proteomes; UP000000601; 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; 3.30.70.660; 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..264
FT /note="tRNA pseudouridine synthase A"
FT /id="PRO_0000057350"
FT ACT_SITE 56
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ SEQUENCE 264 AA; 30607 MW; 160D50B0B596C261 CRC64;
MYKECFKIAL GIEYNGSNYH GWQYQKFASS VQEKVELALS IIANHPVRVT CAGRTDAGVH
STGQVVHFCT SSIRNDQAWI LGTNRYLPKD ISVIWKRDVP MHFHARYSAL SRRYRYILYN
NSCRSSIFYQ GLKFYHRILN VEKMNQAAQY LLGEHDFTTF RSSHCQSKTP FRKILYVNVF
CINCLIIIDI VANSFLYHMV RNIVGCLIEI GISKKKVTWI RDILKFKNRT SSTKIVESNG
LYLVQVQYSS LFKLPICPVG PFFV
//
