TRUB_MYCTU
ID TRUB_MYCTU Reviewed; 298 AA.
AC P9WHP7; L0TDK3; O33335; P62190;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
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=MTB-TRUB;
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=Rv2793c;
GN ORFNames=MTV002.58c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15028724; DOI=10.1074/jbc.m401045200;
RA Chaudhuri B.N., Chan S., Perry L.J., Yeates T.O.;
RT "Crystal structure of the apo forms of psi 55 tRNA pseudouridine synthase
RT from Mycobacterium tuberculosis: a hinge at the base of the catalytic
RT cleft.";
RL J. Biol. Chem. 279:24585-24591(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP45592.1; -; Genomic_DNA.
DR PIR; H70884; H70884.
DR RefSeq; NP_217309.1; NC_000962.3.
DR RefSeq; WP_003414147.1; NZ_NVQJ01000020.1.
DR PDB; 1SGV; X-ray; 1.90 A; A/B=1-298.
DR PDBsum; 1SGV; -.
DR AlphaFoldDB; P9WHP7; -.
DR SMR; P9WHP7; -.
DR STRING; 83332.Rv2793c; -.
DR PaxDb; P9WHP7; -.
DR DNASU; 888587; -.
DR GeneID; 888587; -.
DR KEGG; mtu:Rv2793c; -.
DR TubercuList; Rv2793c; -.
DR eggNOG; COG0130; Bacteria.
DR OMA; ELQFIRW; -.
DR PhylomeDB; P9WHP7; -.
DR BRENDA; 5.4.99.25; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
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; IPR015225; tRNA_psdUridine_synth_fam2_C.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR InterPro; IPR032819; TruB_C.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF09142; TruB_C; 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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome; tRNA processing.
FT CHAIN 1..298
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_0000121872"
FT ACT_SITE 42
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:1SGV"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:1SGV"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:1SGV"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1SGV"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 148..161
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:1SGV"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:1SGV"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1SGV"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1SGV"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1SGV"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:1SGV"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:1SGV"
SQ SEQUENCE 298 AA; 31820 MW; 9F77797DC13B34C6 CRC64;
MSATGPGIVV IDKPAGMTSH DVVGRCRRIF ATRRVGHAGT LDPMATGVLV IGIERATKIL
GLLTAAPKSY AATIRLGQTT STEDAEGQVL QSVPAKHLTI EAIDAAMERL RGEIRQVPSS
VSAIKVGGRR AYRLARQGRS VQLEARPIRI DRFELLAARR RDQLIDIDVE IDCSSGTYIR
ALARDLGDAL GVGGHVTALR RTRVGRFELD QARSLDDLAE RPALSLSLDE ACLLMFARRD
LTAAEASAAA NGRSLPAVGI DGVYAACDAD GRVIALLRDE GSRTRSVAVL RPATMHPG
