TRUD_CELJU
ID TRUD_CELJU Reviewed; 336 AA.
AC B3PJA9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=CJA_2221;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(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; CP000934; ACE84664.1; -; Genomic_DNA.
DR RefSeq; WP_012487821.1; NC_010995.1.
DR AlphaFoldDB; B3PJA9; -.
DR SMR; B3PJA9; -.
DR STRING; 498211.CJA_2221; -.
DR PRIDE; B3PJA9; -.
DR EnsemblBacteria; ACE84664; ACE84664; CJA_2221.
DR KEGG; cja:CJA_2221; -.
DR eggNOG; COG0585; Bacteria.
DR HOGENOM; CLU_005281_4_0_6; -.
DR OMA; LWLWVEK; -.
DR OrthoDB; 1490777at2; -.
DR Proteomes; UP000001036; 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; 3.30.2350.20; -; 2.
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 Pfam; PF01142; TruD; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR PROSITE; PS50984; TRUD; 1.
DR PROSITE; PS01268; UPF0024; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; tRNA processing.
FT CHAIN 1..336
FT /note="tRNA pseudouridine synthase D"
FT /id="PRO_1000149841"
FT DOMAIN 164..298
FT /note="TRUD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
SQ SEQUENCE 336 AA; 38220 MW; B27D800AF27C56F3 CRC64;
MRIQADFSLD FPRAYGTLEA SADFRTVPED FQVTENLGFE PAGEGEHVYL WIEKRGENTA
WVAEQLAVYA GVKPTDIGYA GRKDRHAITR QWFSVYLPLK SNHPEPEWQG FSSDRIQVLR
VARHVRKLRR GEHESNHFVI GLRQLQCADK TAFHERLDCV LRSGVPNYFG EQRFGNAGRN
LIEAESLLVG KKPYRDRQKR GLILSAARSY LFNQVLADRV RKGDWQISVA GEPCAYPSGP
LWGRGRPLAL VELLARETEL LSSWRDWCNE LEHVGTSQER RALLLAIKTP SYRWLVGDHL
ELAFTLEAGA FATSVLRELV SLNNQQLRLS GTESSD