ID   TRUB_GLUOX              Reviewed;         333 AA.
AC   Q5FQM1;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=GOX1584;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW61325.1; -; Genomic_DNA.
DR   RefSeq; WP_011253109.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FQM1; -.
DR   SMR; Q5FQM1; -.
DR   STRING; 290633.GOX1584; -.
DR   EnsemblBacteria; AAW61325; AAW61325; GOX1584.
DR   KEGG; gox:GOX1584; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_3_5; -.
DR   OMA; ELQFIRW; -.
DR   Proteomes; UP000006375; 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..333
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_0000121841"
FT   ACT_SITE        46
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   333 AA;  36318 MW;  91403B8B6D6194B0 CRC64;
     MGRKRGRDID GWLILDKPLG PTSTDMVNKL RWAFDAKKAG HGGTLDPLAS GVLPIAFGKA
     TRTIPYIMDA TKRYRFTLTF GESRTTDDLE GEVLATSPNR PTDDQIRAVL PALTGNVMQV
     PPVFSALRVG GERAYDMARA GRPPELPPRP ARIDSITLVE RPDANTAVFD VQSGKGVYMR
     SLARDIALAC GTVGHISVLR RTKCGPFDLS HALTIDQISL DKSTQTVDNA DALPAPLLDA
     ATALVDIPAL AVTDAEGRML VWGQSIDPAD LVHPLPASSQ GEDHLWRAMI GEHVLGLCHV
     RHGRLRAARM LENHEFFGEH DVDYRRTPHG TDF