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
//