TRUD_SALG2
ID TRUD_SALG2 Reviewed; 349 AA.
AC B5RDQ1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=tRNA pseudouridine synthase D {ECO:0000255|HAMAP-Rule:MF_01082};
DE EC=5.4.99.27 {ECO:0000255|HAMAP-Rule:MF_01082};
DE AltName: Full=tRNA pseudouridine(13) synthase {ECO:0000255|HAMAP-Rule:MF_01082};
DE AltName: Full=tRNA pseudouridylate synthase D {ECO:0000255|HAMAP-Rule:MF_01082};
DE AltName: Full=tRNA-uridine isomerase D {ECO:0000255|HAMAP-Rule:MF_01082};
GN Name=truD {ECO:0000255|HAMAP-Rule:MF_01082}; OrderedLocusNames=SG2831;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-13 in
CC transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(13) in tRNA = pseudouridine(13) in tRNA;
CC Xref=Rhea:RHEA:42540, Rhea:RHEA-COMP:10105, Rhea:RHEA-COMP:10106,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01082};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC {ECO:0000255|HAMAP-Rule:MF_01082}.
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DR EMBL; AM933173; CAR38639.1; -; Genomic_DNA.
DR RefSeq; WP_000134246.1; NC_011274.1.
DR AlphaFoldDB; B5RDQ1; -.
DR SMR; B5RDQ1; -.
DR EnsemblBacteria; CAR38639; CAR38639; SG2831.
DR KEGG; seg:SG2831; -.
DR HOGENOM; CLU_005281_4_0_6; -.
DR OMA; LWLWVEK; -.
DR Proteomes; UP000008321; 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 Gene3D; 3.30.2340.10; -; 1.
DR Gene3D; 3.30.2350.20; -; 1.
DR HAMAP; MF_01082; TruD; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001656; PsdUridine_synth_TruD.
DR InterPro; IPR020119; PsdUridine_synth_TruD_CS.
DR InterPro; IPR011760; PsdUridine_synth_TruD_insert.
DR InterPro; IPR042214; TruD_catalytic.
DR InterPro; IPR043165; TruD_insert_sf.
DR Pfam; PF01142; TruD; 2.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1.
DR PROSITE; PS50984; TRUD; 1.
DR PROSITE; PS01268; UPF0024; 1.
PE 3: Inferred from homology;
KW Isomerase; tRNA processing.
FT CHAIN 1..349
FT /note="tRNA pseudouridine synthase D"
FT /id="PRO_1000136850"
FT DOMAIN 155..303
FT /note="TRUD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
SQ SEQUENCE 349 AA; 39333 MW; 5357437747CD5A51 CRC64;
MTEFDNLTWL HGKPQGSGLL KANPEDFVVV EDLGFTPDGE GEHILLRILK NGCNTRFVAD
ALAKFLKIHA REVSFAGQKD KHAVTEQWLC ARVPGKEMPD FSAFQLEGCK VLEYARHKRK
LRLGALKGNA FTLVLREISD RRDVETRLQA IRDGGVPNYF GAQRFGIGGS NLQGALRWAQ
SNAPVRDRNK RSFWLSAARS ALFNQIVHQR LKKPDFNQVV DGDALQLAGR GSWFVATSEE
LPELQRRVDE KELMITASLP GSGEWGTQRA ALAFEQDAIA QETVLQSLLL REKVEASRRA
MLLYPQQLSW NWWDDVTVEL RFWLPAGSFA TSVVRELINT MGDYAHIAE