ID   TRUB_PROM0              Reviewed;         305 AA.
AC   A3PEI1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=P9301_15331;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
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; CP000576; ABO18156.1; -; Genomic_DNA.
DR   RefSeq; WP_011863460.1; NC_009091.1.
DR   AlphaFoldDB; A3PEI1; -.
DR   SMR; A3PEI1; -.
DR   STRING; 167546.P9301_15331; -.
DR   EnsemblBacteria; ABO18156; ABO18156; P9301_15331.
DR   KEGG; pmg:P9301_15331; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_0_3; -.
DR   OMA; ELQFIRW; -.
DR   Proteomes; UP000001430; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..305
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084637"
FT   ACT_SITE        41
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   305 AA;  34672 MW;  C83FEB8B31812ABE CRC64;
     METKDGFLVI NKDKGCTSHD CVKQIRKLLN TKKVGHTGTL DPEVIGILPI AIGSATRFIQ
     YLPQGKTYIG QIKLGIRTNT DDIHGEIINQ KSWPKISDEK LDQYLNRFRG IIKQIPPKVS
     SVHINGERAY KKSFRNEVFE LAPREVKIDE LTLMKWDQIN GILEIKVKCS AGTYIRAIAR
     DLGEILNSEG CLLQLKRISA CGFDEQNSIK ISDIEKDKKN SKNFIIPTIS ALNHISSFVL
     STEEQINFWQ TGRAIRVDIN YFQENKSFDY KKPIKVIDKK QILLGIGFLN EEQSNINPKL
     VLNAK