ID TRUB_PELTS Reviewed; 316 AA.
AC A5D2S3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=PTH_1272;
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI;
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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; AP009389; BAF59453.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D2S3; -.
DR SMR; A5D2S3; -.
DR STRING; 370438.PTH_1272; -.
DR KEGG; pth:PTH_1272; -.
DR eggNOG; COG0130; Bacteria.
DR HOGENOM; CLU_032087_0_1_9; -.
DR Proteomes; UP000006556; 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 CDD; cd07953; PUA; 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; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR InterPro; IPR032819; TruB_C.
DR NCBIfam; TIGR00431; TruB; 1.
DR PANTHER; PTHR13767:SF2; PSEUDOURIDYLATE SYNTHASE TRUB1; 1.
DR PANTHER; PTHR13767; TRNA-PSEUDOURIDINE SYNTHASE; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; tRNA processing.
FT CHAIN 1..316
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_1000084636"
FT DOMAIN 238..312
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
FT ACT_SITE 38
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ SEQUENCE 316 AA; 34462 MW; F74FB6898815205D CRC64;
MNGIVNVLKP PGMSSHDVVD RIRRIFGVKK AGHTGTLDPG AAGVLVVCLG VATRLARFLL
GEDKEYRVEI TFGMSTSTGD SYGEITDQRD ASFLKEHDII RVLPEFTGEV RQVPPMTSAI
KWRGKKLYEL AREGLVVERQ ERAVYIKSLE FIRGSGWGTP SPRALMHLSC SKGTYVRSLC
HDMGSRLGCG AHMSFLVRTR AGPFKIADSV TLEELQAAAS KGVLERKIIE MDRAVSEYPE
VIVKSSAVKA VAAGSKLYIP GVARMPLDLD CGKLVRLTGP DGLLAIAEAG REPFDKEKLF
FKPVCVLARQ AGRSSN
//
