TRUA_BURM1
ID TRUA_BURM1 Reviewed; 270 AA.
AC Q83WJ5; A9AMA9;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Bmul_4624, BMULJ_03887;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12754231; DOI=10.1128/jb.185.11.3333-3343.2003;
RA Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.;
RT "Distribution and organization of auxotrophic genes on the multichromosomal
RT genome of Burkholderia multivorans ATCC 17616.";
RL J. Bacteriol. 185:3333-3343(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; AB091435; BAC65262.1; -; Genomic_DNA.
DR EMBL; CP000869; ABX18302.1; -; Genomic_DNA.
DR EMBL; AP009386; BAG45747.1; -; Genomic_DNA.
DR RefSeq; WP_012217297.1; NC_010805.1.
DR AlphaFoldDB; Q83WJ5; -.
DR SMR; Q83WJ5; -.
DR STRING; 395019.Bmul_4624; -.
DR EnsemblBacteria; BAG45747; BAG45747; BMULJ_03887.
DR KEGG; bmj:BMULJ_03887; -.
DR KEGG; bmu:Bmul_4624; -.
DR eggNOG; COG0101; Bacteria.
DR HOGENOM; CLU_014673_0_2_4; -.
DR OMA; FLYGMVR; -.
DR Proteomes; UP000008815; Chromosome 2.
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_0000057352"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ SEQUENCE 270 AA; 30094 MW; 4BB9E5DBE397C07F CRC64;
MRIALGIQYD GAAFCGWQAQ PHGNTVQDAL ERALAEFARV PLHTTVAGRT DTGVHGLGQV
VHFDTELDRA DFSWVRGTNA FLPPTVAVQW AKSMPDAFHA RFSAFERTYY YALYVHPVRS
PMLDGRAGWI HTPLDDDAMR AAAAHLLGEH DFSAFRSSEC QSKTPVKHLY EIDIRRVGHF
LHFRFRANAF LHHMVRNLMG CLVAVGRGRY PADWVADVLA GRDRNRAAPT FMADGLYLAH
VGYPAEFAVP PAQLGSVPWS SVWADLDPQP
