ID   TRUB_PROM2              Reviewed;         305 AA.
AC   A8G6F8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=P9215_15761;
OS   Prochlorococcus marinus (strain MIT 9215).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9215;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000825; ABV51189.1; -; Genomic_DNA.
DR   RefSeq; WP_012008227.1; NC_009840.1.
DR   AlphaFoldDB; A8G6F8; -.
DR   SMR; A8G6F8; -.
DR   STRING; 93060.P9215_15761; -.
DR   EnsemblBacteria; ABV51189; ABV51189; P9215_15761.
DR   KEGG; pmh:P9215_15761; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_0_3; -.
DR   OMA; ELQFIRW; -.
DR   OrthoDB; 1166299at2; -.
DR   Proteomes; UP000002014; 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   PANTHER; PTHR13767; PTHR13767; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00431; TruB; 1.
PE   3: Inferred from homology;
KW   Isomerase; tRNA processing.
FT   CHAIN           1..305
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084639"
FT   ACT_SITE        41
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   305 AA;  34550 MW;  9667FF5751399E5C CRC64;
     METNDGFLVI NKDKGCTSHD CVKQIRKLLN TKKVGHTGTL DPEVIGTLPI AIGSATRFIQ
     YLPQSKTYIG KIKLGIRTNT DDIHGEIINQ KSWPKISEEK LDQYLKRFRG IIKQVPPKVS
     SVHVNGERAY KKSFRNEIFE LAPREVKIKE LTLMKWDQIN GIITIKIKCS SGTYIRAIAR
     DLGGILNSEG CLLQLKRISA CGFDEQSSIK ISDIEKAKKN APKFIIPTIS ALDHISTYSL
     NKDEEINYWQ TGRAIKIDIN FLYECKAFDY KQPLKVVDSR KMLLGIGFLD DDHTKINPKL
     VLNAK