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Database: UniProt
Entry: D6ZW90_BIFLJ
LinkDB: D6ZW90_BIFLJ
Original site: D6ZW90_BIFLJ 
ID   D6ZW90_BIFLJ            Unreviewed;       387 AA.
AC   D6ZW90;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=tRNA pseudouridine synthase B {ECO:0000256|HAMAP-Rule:MF_01080};
DE            EC=5.4.99.25 {ECO:0000256|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE            Short=Psi55 synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA pseudouridylate synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA-uridine isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
GN   Name=truB {ECO:0000256|HAMAP-Rule:MF_01080};
GN   OrderedLocusNames=BLJ_1713 {ECO:0000313|EMBL:ADH01146.1};
OS   Bifidobacterium longum subsp. longum (strain JDM301).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=759350 {ECO:0000313|EMBL:ADH01146.1, ECO:0000313|Proteomes:UP000006740};
RN   [1] {ECO:0000313|EMBL:ADH01146.1, ECO:0000313|Proteomes:UP000006740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM301 {ECO:0000313|EMBL:ADH01146.1,
RC   ECO:0000313|Proteomes:UP000006740};
RX   PubMed=20525832; DOI=10.1128/JB.00538-10;
RA   Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P.,
RA   Wang S., Guo X.K.;
RT   "Complete genome sequence of Bifidobacterium longum JDM301.";
RL   J. Bacteriol. 192:4076-4077(2010).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in
CC       the psi GC loop of transfer RNAs. {ECO:0000256|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:0000256|ARBA:ARBA00000385, ECO:0000256|HAMAP-
CC         Rule:MF_01080};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00005642, ECO:0000256|HAMAP-
CC       Rule:MF_01080}.
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DR   EMBL; CP002010; ADH01146.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6ZW90; -.
DR   KEGG; bll:BLJ_1713; -.
DR   HOGENOM; CLU_032087_0_0_11; -.
DR   Proteomes; UP000006740; 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; 3.30.2350.10; Pseudouridine synthase; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 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:SF2; PSEUDOURIDYLATE SYNTHASE TRUB1; 1.
DR   PANTHER; PTHR13767; TRNA-PSEUDOURIDINE SYNTHASE; 1.
DR   Pfam; PF09142; TruB_C; 1.
DR   Pfam; PF16198; TruB_C_2; 1.
DR   Pfam; PF01509; TruB_N; 2.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01080}.
FT   DOMAIN          29..94
FT                   /note="Pseudouridine synthase II N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01509"
FT   DOMAIN          114..224
FT                   /note="Pseudouridine synthase II N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01509"
FT   DOMAIN          225..258
FT                   /note="tRNA pseudouridylate synthase B C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16198"
FT   DOMAIN          329..385
FT                   /note="tRNA pseudouridine synthase II TruB subfamily 2 C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09142"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   387 AA;  41817 MW;  E92777111585095E CRC64;
     MLHTTPSGLL IIDKPQGVTS FDAVAAVRGA LHIKKVGHAG TLDPMATGTL VIAFGHATRL
     LNAIMAHDKT YEATIRLGLR TTTDDAEGEV LVDDEARSRW QTLSAQLTEG GQSGEPTALP
     TASWQDLLTR TIATNFTGDI EQVPNTFSAI KINGQRAYDL AREGKEVELK PRPVTISEFT
     VLNIRSGFVA GEQAAEPLRE DANTGTIPAL DIDVRVSCSS GTYIRALARD LGNELGVGGY
     LTRLRRTRVG RFALPDDTSG LIASEAMLDT RTHTVTAHTD QKTFTNREGQ TVTRNKCVLN
     TPEGLAGDER RNWLLDHALT MEQAARGAMP ALDITPEEAS ELRFGRRIER AISESTAAIV
     PQTHDVAAII ERANAHQAKP VTVFPLA
//
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