ID TRUB_THEMA Reviewed; 309 AA. AC Q9WZW0; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 154. 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, ECO:0000303|PubMed:12499554}; 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, GN ECO:0000303|PubMed:14566049}; OrderedLocusNames=TM_0856; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CRYSTALLIZATION. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=12499554; DOI=10.1107/s0907444902018292; RA Wouters J., Tricot C., Durbecq V., Roovers M., Stalon V., Droogmans L.; RT "Preliminary X-ray crystallographic analysis of tRNA pseudouridine 55 RT synthase from the thermophilic eubacterium Thermotoga maritima."; RL Acta Crystallogr. D 59:152-154(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF COMPLEX WITH RNA. RX PubMed=14566049; DOI=10.1073/pnas.2135585100; RA Pan H., Agarwalla S., Moustakas D.T., Finer-Moore J., Stroud R.M.; RT "Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA RT recognition through a combination of rigid docking and induced fit."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12648-12653(2003). 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; AE000512; AAD35938.1; -; Genomic_DNA. DR PIR; A72325; A72325. DR RefSeq; NP_228665.1; NC_000853.1. DR RefSeq; WP_004080766.1; NZ_CP011107.1. DR PDB; 1R3E; X-ray; 2.10 A; A=1-309. DR PDB; 1ZE1; X-ray; 2.90 A; A/B/C/D=1-309. DR PDB; 1ZE2; X-ray; 3.00 A; A/B=1-309. DR PDB; 2AB4; X-ray; 2.40 A; A=1-309. DR PDBsum; 1R3E; -. DR PDBsum; 1ZE1; -. DR PDBsum; 1ZE2; -. DR PDBsum; 2AB4; -. DR AlphaFoldDB; Q9WZW0; -. DR SMR; Q9WZW0; -. DR STRING; 243274.TM_0856; -. DR PaxDb; 243274-THEMA_00355; -. DR EnsemblBacteria; AAD35938; AAD35938; TM_0856. DR KEGG; tma:TM0856; -. DR eggNOG; COG0130; Bacteria. DR InParanoid; Q9WZW0; -. DR OrthoDB; 9802309at2; -. DR BRENDA; 5.4.99.25; 6331. DR EvolutionaryTrace; Q9WZW0; -. DR Proteomes; UP000008183; Chromosome. 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 CDD; cd21905; PUA_TruB_thermotogae; 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; IPR002478; PUA. 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; PF01472; PUA; 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 1: Evidence at protein level; KW 3D-structure; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1..309 FT /note="tRNA pseudouridine synthase B" FT /id="PRO_0000121929" FT DOMAIN 229..306 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080" FT ACT_SITE 39 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080" FT STRAND 4..10 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:1R3E" FT HELIX 16..26 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 32..36 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 43..50 FT /evidence="ECO:0007829|PDB:1R3E" FT HELIX 51..60 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 65..73 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:1R3E" FT HELIX 96..104 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 105..112 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:2AB4" FT HELIX 127..132 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:1ZE1" FT STRAND 142..155 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 158..165 FT /evidence="ECO:0007829|PDB:1R3E" FT HELIX 171..181 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 186..196 FT /evidence="ECO:0007829|PDB:1R3E" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:1R3E" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:1R3E" FT HELIX 212..218 FT /evidence="ECO:0007829|PDB:1R3E" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:1R3E" FT TURN 236..238 FT /evidence="ECO:0007829|PDB:1R3E" FT HELIX 239..242 FT /evidence="ECO:0007829|PDB:1R3E" FT TURN 243..245 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 248..252 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:1ZE1" FT STRAND 264..268 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:1R3E" FT STRAND 274..282 FT /evidence="ECO:0007829|PDB:1R3E" FT HELIX 287..290 FT /evidence="ECO:0007829|PDB:1ZE1" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:1ZE1" FT STRAND 298..305 FT /evidence="ECO:0007829|PDB:1R3E" SQ SEQUENCE 309 AA; 35459 MW; 04825FD6D643CE9C CRC64; MKHGILVAYK PKGPTSHDVV DEVRKKLKTR KVGHGGTLDP FACGVLIIGV NQGTRILEFY KDLKKVYWVK MRLGLITETF DITGEVVEER ECNVTEEEIR EAIFSFVGEY DQVPPAYSAK KYKGERLYKL AREGKIINLP PKRVKIFKIW DVNIEGRDVS FRVEVSPGTY IRSLCMDIGY KLGCGATAVE LVRESVGPHT IEESLNVFEA APEEIENRII PLEKCLEWLP RVVVHQESTK MILNGSQIHL EMLKEWDGFK KGEVVRVFNE EGRLLALAEA ERNSSFLETL RKHERNERVL TLRKVFNTR //