TRUB_BLOFL
ID TRUB_BLOFL Reviewed; 255 AA.
AC P59877;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Bfl106;
OS Blochmannia floridanus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=203907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83627.1; -; Genomic_DNA.
DR RefSeq; WP_011126396.1; NC_005061.1.
DR AlphaFoldDB; P59877; -.
DR SMR; P59877; -.
DR STRING; 203907.Bfl106; -.
DR PRIDE; P59877; -.
DR EnsemblBacteria; CAD83627; CAD83627; Bfl106.
DR KEGG; bfl:Bfl106; -.
DR eggNOG; COG0130; Bacteria.
DR HOGENOM; CLU_032087_2_0_6; -.
DR OMA; ELQFIRW; -.
DR OrthoDB; 1166299at2; -.
DR Proteomes; UP000002192; 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 HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR InterPro; IPR032819; TruB_C.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00431; TruB; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; tRNA processing.
FT CHAIN 1..255
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_0000121813"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ SEQUENCE 255 AA; 29037 MW; 3CBECC765578583D CRC64;
MQRYVNFFDK NRRDVHGLLL LDKPTGFSSS FFLNKIKKLF YAKKVGYIGT LDPIATGMLP
ICFGKATKFA SYLLNSDKRY RVLVKLGEST DTFDASGVII RIADVQCNKE KIEECLKSFL
GTSLQIPPMF SSLKYQGLPL YKYARRGVNI PRKSRTIHVY SLYCLNQLNS IIELEIHCSK
GTYVRSIVND IGEYLGCGAH IISLRRLMVG QYIASMMVNI KTIESIFFDK DLNDLEVLDK
LDNLLISTET IMCSF
