TRUB_BIFLD
ID TRUB_BIFLD Reviewed; 387 AA.
AC B3DQF2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01080};
DE EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01080};
GN Name=truB {ECO:0000255|HAMAP-Rule:MF_01080}; OrderedLocusNames=BLD_1745;
OS Bifidobacterium longum (strain DJO10A).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=205913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A;
RX PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT reveals loci susceptible to deletion during pure culture growth.";
RL BMC Genomics 9:247-247(2008).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in
CC the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01080};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01080}.
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DR EMBL; CP000605; ACD99190.1; -; Genomic_DNA.
DR RefSeq; WP_007053815.1; NZ_AABM02000016.1.
DR AlphaFoldDB; B3DQF2; -.
DR SMR; B3DQF2; -.
DR EnsemblBacteria; ACD99190; ACD99190; BLD_1745.
DR GeneID; 66505894; -.
DR KEGG; blj:BLD_1745; -.
DR HOGENOM; CLU_032087_0_0_11; -.
DR OMA; HVETREY; -.
DR Proteomes; UP000002419; 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; cd02573; PseudoU_synth_EcTruB; 1.
DR Gene3D; 2.30.130.10; -; 1.
DR HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR015225; tRNA_psdUridine_synth_fam2_C.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR InterPro; IPR032819; TruB_C.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF09142; TruB_C; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 2.
DR SUPFAM; SSF55120; SSF55120; 1.
PE 3: Inferred from homology;
KW Isomerase; tRNA processing.
FT CHAIN 1..387
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_1000136808"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ SEQUENCE 387 AA; 41807 MW; 85C79E9252D07197 CRC64;
MLHTTPSGLL IIDKPQGVTS FDAVAAVRGA LHIKKVGHAG TLDPMATGTL VIAFGHATRL
LNAIVAHDKT YEATIRLGLR TTTDDAEGEV LVDDEARSRW QTLSAQLTEG GQSGEPTALP
TASWQDLLTR TIATNFTGDI EQVPNTFSAI KINGQRAYDL AREGKDVELK PRPVTISEFT
VLDIRSGFVA GEQTAEPLRE DANTGAIPAL DVDVRISCSS GTYIRALARD LGKELGVGGY
LTRLRRTRVG RFALPDDASG LIAPEAMLDT RTHTVTAHTD QKTFTNREGQ TVTRNKCVLD
TPEGLAGDER RNWLLDHALT MEQAARGAMP ALDITPEEAS ELRFGRRIER TISEPTAAIV
PQTHDVAAII ERANAHQAKP VTVFPLA
