ID TRPB1_THEMA Reviewed; 389 AA. AC P50909; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 160. DE RecName: Full=Tryptophan synthase beta chain 1; DE EC=4.2.1.20; GN Name=trpB1; Synonyms=trpB; OrderedLocusNames=TM_0138; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales; OC Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7556082; DOI=10.1002/j.1460-2075.1995.tb00118.x; RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.; RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the RT hyperthermophile Thermotoga maritima."; RL EMBO J. 14:4395-4402(1995). RN [2] 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). CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L- CC tryptophan from indole and L-serine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D- CC glyceraldehyde 3-phosphate + L-tryptophan + H2O; CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}. 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; X92729; CAA63391.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35231.1; -; Genomic_DNA. DR PIR; S59049; S59049. DR RefSeq; WP_004082734.1; NC_000853.1. DR PDB; 8EGY; X-ray; 2.05 A; A/B=1-389. DR PDB; 8EGZ; X-ray; 1.90 A; A/B=1-389. DR PDB; 8EH0; X-ray; 1.70 A; A/B=1-389. DR PDB; 8EH1; X-ray; 2.00 A; A/B=1-389. DR PDB; 8VHH; X-ray; 2.15 A; A/B=1-389. DR AlphaFoldDB; P50909; -. DR SMR; P50909; -. DR FunCoup; P50909; 371. DR STRING; 243274.TM_0138; -. DR PaxDb; 243274-TM_0138; -. DR EnsemblBacteria; AAD35231; AAD35231; TM_0138. DR KEGG; tma:TM0138; -. DR KEGG; tmi:THEMA_04115; -. DR KEGG; tmm:Tmari_0136; -. DR KEGG; tmw:THMA_0133; -. DR eggNOG; COG0133; Bacteria. DR InParanoid; P50909; -. DR OrthoDB; 9766131at2; -. DR BioCyc; MetaCyc:MONOMER-345; -. DR BRENDA; 4.2.1.20; 6331. DR SABIO-RK; P50909; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000162; P:L-tryptophan biosynthetic process; IBA:GO_Central. DR CDD; cd06446; Trp-synth_B; 1. DR FunFam; 3.40.50.1100:FF:000001; Tryptophan synthase beta chain; 1. DR FunFam; 3.40.50.1100:FF:000004; Tryptophan synthase beta chain; 1. DR Gene3D; 3.40.50.1100; -; 2. DR HAMAP; MF_00133; Trp_synth_beta; 1. DR InterPro; IPR006653; Trp_synth_b_CS. DR InterPro; IPR006654; Trp_synth_beta. DR InterPro; IPR023026; Trp_synth_beta/beta-like. DR InterPro; IPR001926; TrpB-like_PALP. DR InterPro; IPR036052; TrpB-like_PALP_sf. DR NCBIfam; TIGR00263; trpB; 1. DR PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1. DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF001413; Trp_syn_beta; 1. DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1. DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1. DR PDBsum; 8EGY; -. DR PDBsum; 8EGZ; -. DR PDBsum; 8EH0; -. DR PDBsum; 8EH1; -. DR PDBsum; 8VHH; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Lyase; Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis. FT CHAIN 1..389 FT /note="Tryptophan synthase beta chain 1" FT /id="PRO_0000099013" FT MOD_RES 83 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250" FT HELIX 17..31 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 35..44 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 45..49 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 59..65 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 67..73 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:8EH1" FT HELIX 83..96 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 101..109 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 110..121 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 125..131 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 132..137 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 139..147 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 151..155 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 162..175 FT /evidence="ECO:0007829|PDB:8EH0" FT TURN 176..179 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 193..201 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 203..216 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 231..237 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 246..252 FT /evidence="ECO:0007829|PDB:8EH0" FT TURN 257..260 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 265..268 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 270..274 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 277..281 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:8EH0" FT TURN 297..299 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 306..313 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 316..322 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 324..338 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 346..351 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 352..355 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 362..367 FT /evidence="ECO:0007829|PDB:8EH0" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 375..379 FT /evidence="ECO:0007829|PDB:8EH0" FT HELIX 382..385 FT /evidence="ECO:0007829|PDB:8EH0" SQ SEQUENCE 389 AA; 42917 MW; 23AF62465A3E1CDE CRC64; MKGYFGPYGG QYVPEILMPA LEELEAAYEE IMKDESFWKE FNDLLRDYAG RPTPLYFARR LSEKYGARIY LKREDLLHTG AHKINNAIGQ VLLAKKMGKT RIIAETGAGQ HGVATATAAA LFGMECVIYM GEEDTIRQKP NVERMKLLGA KVVPVKSGSR TLKDAINEAL RDWITNLQTT YYVIGSVVGP HPYPIIVRNF QKVIGEETKK QILEKEGRLP DYIVACVGGG SNAAGIFYPF IDSGVKLIGV EAGGEGLETG KHAASLLKGK IGYLHGSKTF VLQDDWGQVQ VTHSVSAGLD YSGVGPEHAY WRETGKVLYD AVTDEEALDA FIELSRLEGI IPALESSHAL AYLKKINIKG KVVVVNLSGR GDKDLESVLN HPYVRERIR //