TRUB_BIFLO
ID TRUB_BIFLO Reviewed; 387 AA.
AC Q8CY45;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=BL1618;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25406.1; -; Genomic_DNA.
DR RefSeq; NP_696770.1; NC_004307.2.
DR RefSeq; WP_011068748.1; NC_004307.2.
DR AlphaFoldDB; Q8CY45; -.
DR SMR; Q8CY45; -.
DR STRING; 206672.BL1618; -.
DR EnsemblBacteria; AAN25406; AAN25406; BL1618.
DR KEGG; blo:BL1618; -.
DR PATRIC; fig|206672.9.peg.1673; -.
DR HOGENOM; CLU_032087_0_0_11; -.
DR OMA; HVETREY; -.
DR PhylomeDB; Q8CY45; -.
DR Proteomes; UP000000439; 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; Reference proteome; tRNA processing.
FT CHAIN 1..387
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_0000121797"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ SEQUENCE 387 AA; 41719 MW; C9C84B4CB84DAAA5 CRC64;
MLHTTPSGLL IIDKPQGVTS FDAVAAVRGA LHIKKVGHAG TLDPMATGTL VIAFGHATRL
LNAIVAHDKT YEATIRLGLR TTTDDAEGEV LVDGEARSRW QTLSAQLTEG GQSGEPTALP
TASWQDLLTR TIATNFTGDI EQVPNTFSAI KINGQRAYDL AREGKDVELK PRPVTISEFT
VLDIRSGFVA GEQAAEPLRE DANTGAIPAL DVDVRISCSS GTYIRALARD LGKELGVGGY
LTRLRRTRVG RFALPDDASG LIAPEAMLDT RTHTVTAHTD QKTFTNREGQ TVTRNKCVLD
TPEGLAGDER RNWLLDHALT MEQAARGAMP ALDITPEEAS ELRFGRRIER TISEPTAAIV
PQTHDVAAII ERANAHQAKP VTVFPLA
