TRUA_CUTAK
ID TRUA_CUTAK Reviewed; 279 AA.
AC Q6A6S8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=PPA1809;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT83535.1; -; Genomic_DNA.
DR RefSeq; WP_002517612.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A6S8; -.
DR SMR; Q6A6S8; -.
DR STRING; 267747.PPA1809; -.
DR EnsemblBacteria; AAT83535; AAT83535; PPA1809.
DR KEGG; pac:PPA1809; -.
DR PATRIC; fig|267747.3.peg.1867; -.
DR eggNOG; COG0101; Bacteria.
DR HOGENOM; CLU_014673_0_2_11; -.
DR OMA; FLYGMVR; -.
DR Proteomes; UP000000603; 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; tRNA processing.
FT CHAIN 1..279
FT /note="tRNA pseudouridine synthase A"
FT /id="PRO_0000057430"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ SEQUENCE 279 AA; 31092 MW; B3A7BE37C580B59A CRC64;
MTRWRLDIAY DGANFSGWAT QPDRRTVQGE LETWIPRVLR LDQPTPLTVA GRTDAGVHAR
GQVAHVDLPD NVDTSAMLRR LSRVLTPDVV VKSVRPVPST FDARFSALWR RYVYRLWDES
SRPDPVTRFH VAPVRGHLDL DRLNTAGTSL LGLRDFAAFC KHREGATTIR TLLDCHAKRL
DDPCGTVEVT VRADAFCHSM VRSLVGALTA VASGRRSQDW LDNVAASTSR ASSVLVMPAC
GLTLEEVGYP SDEDLAQRAA QARSRRSHND ICDTCWEDR
