TRUB_HALHL
ID TRUB_HALHL Reviewed; 304 AA.
AC A1WXU9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=Hhal_1747;
OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS halophila (strain DSM 244 / SL1)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=349124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA Richardson P.;
RT "Complete sequence of Halorhodospira halophila SL1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000544; ABM62511.1; -; Genomic_DNA.
DR RefSeq; WP_011814533.1; NC_008789.1.
DR AlphaFoldDB; A1WXU9; -.
DR SMR; A1WXU9; -.
DR STRING; 349124.Hhal_1747; -.
DR EnsemblBacteria; ABM62511; ABM62511; Hhal_1747.
DR KEGG; hha:Hhal_1747; -.
DR eggNOG; COG0130; Bacteria.
DR HOGENOM; CLU_032087_0_3_6; -.
DR OMA; ELQFIRW; -.
DR OrthoDB; 1166299at2; -.
DR Proteomes; UP000000647; 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 Gene3D; 2.30.130.10; -; 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; IPR015240; tRNA_sdUridine_synth_fam1_C.
DR InterPro; IPR032819; TruB_C.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF09157; TruB-C_2; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00431; TruB; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; tRNA processing.
FT CHAIN 1..304
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_1000149823"
FT ACT_SITE 47
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ SEQUENCE 304 AA; 33133 MW; 548F558BEA4F0369 CRC64;
MAKRRGGRNV TGVLLFDKPA GVTSNKALQQ VKRLFGARKA GHTGSLDPLA TGLLPICFGD
ATKVSGFLLD ADKRYVVTCK LGVATDTGDA EGTERDRAEV PALDEEAVER GLTGFRGPID
QLPPMYSAIK HQGQRLYDLA RQGVEVEREP RRVEIYDLQL VAVRGDELEL SVHCSKGTYI
RTLAEDIAQA LGTVGHVCAL RRLGLGPYQD PAMWTEEMLA ARAEQGREAL DATLLPMDSA
LQQYTGVELA DDLAYFVVQG QPVFVPKAPS EGWLRLYDRG GNFLGMGQAL DDGRIGPKRL
VARR