TRUA_AZOPC
ID TRUA_AZOPC Reviewed; 249 AA.
AC B6YQE4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=CFPG_153;
OS Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC Candidatus Azobacteroides.
OX NCBI_TaxID=511995;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19008447; DOI=10.1126/science.1165578;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT protist cells in termite gut.";
RL Science 322:1108-1109(2008).
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; AP010656; BAG83416.1; -; Genomic_DNA.
DR RefSeq; WP_012573177.1; NC_011565.1.
DR AlphaFoldDB; B6YQE4; -.
DR SMR; B6YQE4; -.
DR STRING; 511995.CFPG_153; -.
DR EnsemblBacteria; BAG83416; BAG83416; CFPG_153.
DR KEGG; aps:CFPG_153; -.
DR eggNOG; COG0101; Bacteria.
DR HOGENOM; CLU_014673_0_1_10; -.
DR OMA; FLYGMVR; -.
DR OrthoDB; 1075262at2; -.
DR Proteomes; UP000000723; 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; 1.
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..249
FT /note="tRNA pseudouridine synthase A"
FT /id="PRO_1000097717"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ SEQUENCE 249 AA; 29004 MW; CA68A9E5B71D80AB CRC64;
MNRYFIYLAY NGRNYCGWQI QPNGITVQQR IQQCLSILLR KSVTIIGAGR TDAGVHANLM
TAHFDWEEIL STTSLTKRLN GILPCDILIY KIIPVKKNAH ARFDAISRKY KYYITYQKNP
FRNEQLFRLK QPLNKHLMNE ASNILSEYSD FTSFCKLHSN TRTNVCRISK AEWNTVQGID
IFTIKADRFL RNMVRSIVGT MIDIGKNKLS ITDFRKIIES KNHIMLKSSV PAHALFLTDI
EYPNWIFKN
