ID TRPB_SALTY Reviewed; 397 AA. AC P0A2K1; P00933; Q56141; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 134. DE RecName: Full=Tryptophan synthase beta chain; DE EC=4.2.1.20; GN Name=trpB; OrderedLocusNames=STM1726; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7007651; DOI=10.1016/0022-2836(80)90259-4; RA Crawford I.P., Nichols B.P., Yanofsky C.; RT "Nucleotide sequence of the trpB gene in Escherichia coli and Salmonella RT typhimurium."; RL J. Mol. Biol. 142:489-502(1980). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 375-397. RX PubMed=388433; DOI=10.1073/pnas.76.10.5244; RA Nichols B.P., Yanofsky C.; RT "Nucleotide sequences of trpA of Salmonella typhimurium and Escherichia RT coli: an evolutionary comparison."; RL Proc. Natl. Acad. Sci. U.S.A. 76:5244-5248(1979). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 375-397. RX PubMed=7017727; DOI=10.1073/pnas.78.4.2169; RA Schneider W.P., Nichols B.P., Yanofsky C.; RT "Procedure for production of hybrid genes and proteins and its use in RT assessing significance of amino acid differences in homologous tryptophan RT synthetase alpha polypeptides."; RL Proc. Natl. Acad. Sci. U.S.A. 78:2169-2173(1981). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12. RX PubMed=381671; DOI=10.1016/0022-2836(79)90422-4; RA Selker E., Yanofsky C.; RT "Nucleotide sequence of the trpC-trpB intercistronic region from Salmonella RT typhimurium."; RL J. Mol. Biol. 130:135-143(1979). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=3053720; DOI=10.1016/s0021-9258(19)77913-7; RA Hyde C.C., Ahmed S.A., Padlan E.A., Miles E.W., Davies D.R.; RT "Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 RT multienzyme complex from Salmonella typhimurium."; RL J. Biol. Chem. 263:17857-17871(1988). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF WILD TYPE AND TYR-87 MUTANTS IN RP COMPLEX WITH L-SERINE, AND PYRIDOXAL PHOSPHATE AT LYS-87. RX PubMed=9201907; DOI=10.1021/bi9700429; RA Rhee S., Parris K.D., Hyde C.C., Ahmed S.A., Miles E.W., Davies D.R.; RT "Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 RT complex with ligands bound to the active sites of the alpha- and beta- RT subunits reveal ligand-induced conformational changes."; RL Biochemistry 36:7664-7680(1997). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=9535826; DOI=10.1074/jbc.273.15.8553; RA Rhee S., Miles E.W., Davies D.R.; RT "Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, RT bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex RT reveals the correct orientation of active site alphaGlu49."; RL J. Biol. Chem. 273:8553-8555(1998). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RA Hyde C.C., Parris K.D., Bhat T.N., Brown C., Ahmed S.A., Miles E.W., RA Davies D.R.; RT "Refined structure of the native form of the tryptophan synthase RT multienzyme complex from Salmonella typhimurium."; RL Submitted (JUL-1998) to the PDB data bank. RN [10] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=10504236; DOI=10.1021/bi9907734; RA Sachpatzidis A., Dealwis C., Lubetsky J.B., Liang P.-H., Anderson K.S., RA Lolis E.; RT "Crystallographic studies of phosphonate-based alpha-reaction transition- RT state analogues complexed to tryptophan synthase."; RL Biochemistry 38:12665-12674(1999). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). RX PubMed=11034989; DOI=10.1074/jbc.c000479200; RA Weyand M., Schlichting I.; RT "Structural basis for the impaired channeling and allosteric inter-subunit RT communication in the beta A169L/beta C170W mutant of tryptophan synthase."; RL J. Biol. Chem. 275:41058-41063(2000). CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L- CC tryptophan from indole and L-serine. CC -!- CATALYTIC ACTIVITY: CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D- CC glyceraldehyde 3-phosphate + H2O + L-tryptophan; 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 -!- 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. CC {ECO:0000269|PubMed:9201907}. CC -!- INTERACTION: CC P0A2K1; P00929: trpA; NbExp=24; IntAct=EBI-1028431, EBI-1028423; CC P0A2K1; P0A2K1: trpB; NbExp=3; IntAct=EBI-1028431, EBI-1028431; 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; V01377; CAA24667.1; -; Genomic_DNA. DR EMBL; J01810; AAA27234.1; -; Genomic_DNA. DR EMBL; AE006468; AAL20644.1; -; Genomic_DNA. DR EMBL; V01376; CAA24665.1; -; Genomic_DNA. DR EMBL; V00364; CAA23661.1; -; Genomic_DNA. DR EMBL; M24299; AAA99293.1; -; Genomic_DNA. DR PIR; A01156; TSEBBT. DR RefSeq; NP_460685.1; NC_003197.2. DR RefSeq; WP_000209485.1; NC_003197.2. DR PDB; 1A50; X-ray; 2.30 A; B=2-397. DR PDB; 1A5A; X-ray; 1.90 A; B=1-395. DR PDB; 1A5B; X-ray; 2.00 A; B=1-395. DR PDB; 1A5S; X-ray; 2.30 A; B=1-397. DR PDB; 1BEU; X-ray; 1.90 A; B=1-395. DR PDB; 1BKS; X-ray; 2.20 A; B=1-397. DR PDB; 1C29; X-ray; 2.30 A; B=1-397. DR PDB; 1C8V; X-ray; 2.20 A; B=1-397. DR PDB; 1C9D; X-ray; 2.30 A; B=1-397. DR PDB; 1CW2; X-ray; 2.00 A; B=1-397. DR PDB; 1CX9; X-ray; 2.30 A; B=1-397. DR PDB; 1FUY; X-ray; 2.25 A; B=2-397. DR PDB; 1K3U; X-ray; 1.70 A; B=2-397. DR PDB; 1K7E; X-ray; 2.30 A; B=2-397. DR PDB; 1K7F; X-ray; 1.90 A; B=2-397. DR PDB; 1K7X; X-ray; 1.70 A; B=2-397. DR PDB; 1K8X; X-ray; 1.90 A; B=1-397. DR PDB; 1K8Y; X-ray; 1.50 A; B=2-397. DR PDB; 1K8Z; X-ray; 1.70 A; B=2-397. DR PDB; 1KFB; X-ray; 1.90 A; B=2-397. DR PDB; 1KFC; X-ray; 1.50 A; B=1-397. DR PDB; 1KFE; X-ray; 1.75 A; B=2-395. DR PDB; 1KFJ; X-ray; 1.80 A; B=1-397. DR PDB; 1KFK; X-ray; 2.40 A; B=1-397. DR PDB; 1QOP; X-ray; 1.40 A; B=2-397. DR PDB; 1QOQ; X-ray; 1.80 A; B=2-397. DR PDB; 1TJP; X-ray; 1.50 A; B=2-397. DR PDB; 1TTP; X-ray; 2.30 A; B=1-397. DR PDB; 1TTQ; X-ray; 2.00 A; B=1-397. DR PDB; 1UBS; X-ray; 1.90 A; B=1-395. DR PDB; 1WBJ; X-ray; 1.50 A; B=2-397. DR PDB; 2CLE; X-ray; 1.50 A; B=2-397. DR PDB; 2CLF; X-ray; 1.70 A; B=2-397. DR PDB; 2CLH; X-ray; 1.70 A; B=2-397. DR PDB; 2CLI; X-ray; 1.70 A; B=2-397. DR PDB; 2CLK; X-ray; 1.50 A; B=2-397. DR PDB; 2CLL; X-ray; 1.60 A; B=2-397. DR PDB; 2CLM; X-ray; 1.51 A; B=2-397. DR PDB; 2CLO; X-ray; 1.50 A; B=2-397. DR PDB; 2J9X; X-ray; 1.90 A; B=2-397. DR PDB; 2J9Y; X-ray; 1.80 A; B=1-397. DR PDB; 2J9Z; X-ray; 1.80 A; B=1-397. DR PDB; 2RH9; X-ray; 1.70 A; B=1-397. DR PDB; 2RHG; X-ray; 2.00 A; B=1-397. DR PDB; 2TRS; X-ray; 2.04 A; B=1-395. DR PDB; 2TSY; X-ray; 2.50 A; B=1-395. DR PDB; 2TYS; X-ray; 1.90 A; B=1-397. DR PDB; 2WSY; X-ray; 3.05 A; B=2-397. DR PDB; 3CEP; X-ray; 2.10 A; B=2-397. DR PDB; 3PR2; X-ray; 1.85 A; B=3-393. DR PDB; 4HN4; X-ray; 1.64 A; B=1-397. DR PDB; 4HPJ; X-ray; 1.45 A; B=1-397. DR PDB; 4HPX; X-ray; 1.65 A; B=1-397. DR PDB; 4HT3; X-ray; 1.30 A; B=1-397. DR PDB; 4KKX; X-ray; 1.77 A; B=1-397. DR PDB; 4WX2; X-ray; 1.75 A; B=1-397. DR PDB; 4XUG; X-ray; 1.65 A; B=1-397. DR PDB; 4Y6G; X-ray; 1.65 A; B=1-397. DR PDB; 4ZQC; X-ray; 1.54 A; B=1-397. DR PDB; 5BW6; X-ray; 1.82 A; B=1-397. DR PDB; 5CGQ; X-ray; 1.18 A; B=1-397. DR PDB; 6C73; X-ray; 1.65 A; B=2-396. DR PDB; 6D0V; X-ray; 1.64 A; B=1-394. DR PDB; 6DUC; X-ray; 1.79 A; B=1-397. DR PDB; 6DZ4; X-ray; 1.45 A; B=1-397. DR PDB; 6DZO; X-ray; 1.64 A; B=2-395. DR PDB; 6O1H; X-ray; 1.64 A; B=2-396. DR PDB; 6VFD; X-ray; 1.70 A; B=1-397. DR PDB; 6VNT; X-ray; 1.25 A; B=1-397. DR PDB; 6WDU; X-ray; 1.40 A; B=1-397. DR PDB; 6WX3; X-ray; 1.20 A; B=1-397. DR PDB; 6X0C; X-ray; 1.45 A; B=1-397. DR PDB; 6XE3; X-ray; 1.55 A; B=1-397. DR PDB; 6XIN; X-ray; 1.75 A; B=1-397. DR PDB; 6XNC; X-ray; 2.11 A; B=1-397. DR PDB; 6XOY; X-ray; 1.64 A; B=1-397. DR PDB; 6XRH; X-ray; 1.44 A; B=1-397. DR PDB; 6XSY; X-ray; 1.55 A; B=1-397. DR PDB; 6XT0; X-ray; 1.37 A; B=1-397. DR PDB; 7A20; X-ray; 2.50 A; A/B/C/D=5-397. DR PDB; 7JHW; X-ray; 1.65 A; B=1-397. DR PDB; 7JLL; X-ray; 1.55 A; B=1-397. DR PDB; 7JMQ; X-ray; 1.60 A; B=1-397. DR PDB; 7JQW; X-ray; 1.70 A; B=1-397. DR PDB; 7JTT; X-ray; 1.64 A; B=1-397. DR PDB; 7K0B; X-ray; 1.57 A; B=1-397. DR PDB; 7K5A; X-ray; 1.50 A; B=1-397. DR PDB; 7KA1; X-ray; 1.60 A; B=1-397. DR PDB; 7KBN; X-ray; 1.60 A; B=1-397. DR PDB; 7KH6; X-ray; 1.45 A; B=1-397. DR PDB; 7KI7; X-ray; 1.75 A; B=1-397. DR PDB; 7KMC; X-ray; 1.50 A; B=1-397. DR PDB; 7KQ9; X-ray; 1.50 A; B=1-397. DR PDB; 7KQF; X-ray; 1.47 A; B=1-397. DR PDB; 7KU9; X-ray; 1.40 A; B=1-397. DR PDB; 7KWV; X-ray; 1.30 A; B=1-397. DR PDB; 7KXC; X-ray; 1.51 A; B=1-397. DR PDB; 7KYT; X-ray; 1.35 A; B=1-397. DR PDB; 7L03; X-ray; 1.60 A; B=1-397. DR PDB; 7L1H; X-ray; 1.50 A; B=1-397. DR PDB; 7L47; X-ray; 1.55 A; B=1-397. DR PDB; 7L4D; X-ray; 1.60 A; B=1-397. DR PDB; 7L5H; X-ray; 1.80 A; B=1-397. DR PDB; 7LEV; X-ray; 1.70 A; B=1-397. DR PDB; 7LGX; X-ray; 1.80 A; B=1-397. DR PDB; 7LKL; X-ray; 1.05 A; B=1-397. DR PDB; 7LPF; X-ray; 1.10 A; B=1-397. DR PDB; 7LT4; X-ray; 1.80 A; B=1-397. DR PDB; 7LTP; X-ray; 1.47 A; B=1-397. DR PDB; 7LUT; X-ray; 1.60 A; B=1-397. DR PDB; 7LV5; X-ray; 1.60 A; B=1-397. DR PDB; 7LVX; X-ray; 1.55 A; B=1-397. DR PDB; 7LX1; X-ray; 1.61 A; B=1-397. DR PDB; 7LY8; X-ray; 1.55 A; B=1-397. DR PDB; 7M2L; X-ray; 1.60 A; B=1-397. DR PDB; 7M3S; X-ray; 1.55 A; B=1-397. DR PDB; 7ME8; X-ray; 1.60 A; B=1-397. DR PDB; 7MT4; X-ray; 1.40 A; B=1-397. DR PDB; 7MT5; X-ray; 1.50 A; B=1-397. DR PDB; 7MT6; X-ray; 1.70 A; B=1-397. DR PDB; 8B03; X-ray; 2.22 A; B=1-397. DR PDB; 8B05; X-ray; 2.10 A; B=1-397. DR PDB; 8B06; X-ray; 2.49 A; B=1-397. DR PDB; 8B08; X-ray; 2.50 A; B=1-397. DR PDBsum; 1A50; -. DR PDBsum; 1A5A; -. DR PDBsum; 1A5B; -. DR PDBsum; 1A5S; -. DR PDBsum; 1BEU; -. DR PDBsum; 1BKS; -. DR PDBsum; 1C29; -. DR PDBsum; 1C8V; -. DR PDBsum; 1C9D; -. DR PDBsum; 1CW2; -. DR PDBsum; 1CX9; -. DR PDBsum; 1FUY; -. DR PDBsum; 1K3U; -. DR PDBsum; 1K7E; -. DR PDBsum; 1K7F; -. DR PDBsum; 1K7X; -. DR PDBsum; 1K8X; -. DR PDBsum; 1K8Y; -. DR PDBsum; 1K8Z; -. DR PDBsum; 1KFB; -. DR PDBsum; 1KFC; -. DR PDBsum; 1KFE; -. DR PDBsum; 1KFJ; -. DR PDBsum; 1KFK; -. DR PDBsum; 1QOP; -. DR PDBsum; 1QOQ; -. DR PDBsum; 1TJP; -. DR PDBsum; 1TTP; -. DR PDBsum; 1TTQ; -. DR PDBsum; 1UBS; -. DR PDBsum; 1WBJ; -. DR PDBsum; 2CLE; -. DR PDBsum; 2CLF; -. DR PDBsum; 2CLH; -. DR PDBsum; 2CLI; -. DR PDBsum; 2CLK; -. DR PDBsum; 2CLL; -. DR PDBsum; 2CLM; -. DR PDBsum; 2CLO; -. DR PDBsum; 2J9X; -. DR PDBsum; 2J9Y; -. DR PDBsum; 2J9Z; -. DR PDBsum; 2RH9; -. DR PDBsum; 2RHG; -. DR PDBsum; 2TRS; -. DR PDBsum; 2TSY; -. DR PDBsum; 2TYS; -. DR PDBsum; 2WSY; -. DR PDBsum; 3CEP; -. DR PDBsum; 3PR2; -. DR PDBsum; 4HN4; -. DR PDBsum; 4HPJ; -. DR PDBsum; 4HPX; -. DR PDBsum; 4HT3; -. DR PDBsum; 4KKX; -. DR PDBsum; 4WX2; -. DR PDBsum; 4XUG; -. DR PDBsum; 4Y6G; -. DR PDBsum; 4ZQC; -. DR PDBsum; 5BW6; -. DR PDBsum; 5CGQ; -. DR PDBsum; 6C73; -. DR PDBsum; 6D0V; -. DR PDBsum; 6DUC; -. DR PDBsum; 6DZ4; -. DR PDBsum; 6DZO; -. DR PDBsum; 6O1H; -. DR PDBsum; 6VFD; -. DR PDBsum; 6VNT; -. DR PDBsum; 6WDU; -. DR PDBsum; 6WX3; -. DR PDBsum; 6X0C; -. DR PDBsum; 6XE3; -. DR PDBsum; 6XIN; -. DR PDBsum; 6XNC; -. DR PDBsum; 6XOY; -. DR PDBsum; 6XRH; -. DR PDBsum; 6XSY; -. DR PDBsum; 6XT0; -. DR PDBsum; 7A20; -. DR PDBsum; 7JHW; -. DR PDBsum; 7JLL; -. DR PDBsum; 7JMQ; -. DR PDBsum; 7JQW; -. DR PDBsum; 7JTT; -. DR PDBsum; 7K0B; -. DR PDBsum; 7K5A; -. DR PDBsum; 7KA1; -. DR PDBsum; 7KBN; -. DR PDBsum; 7KH6; -. DR PDBsum; 7KI7; -. DR PDBsum; 7KMC; -. DR PDBsum; 7KQ9; -. DR PDBsum; 7KQF; -. DR PDBsum; 7KU9; -. DR PDBsum; 7KWV; -. DR PDBsum; 7KXC; -. DR PDBsum; 7KYT; -. DR PDBsum; 7L03; -. DR PDBsum; 7L1H; -. DR PDBsum; 7L47; -. DR PDBsum; 7L4D; -. DR PDBsum; 7L5H; -. DR PDBsum; 7LEV; -. DR PDBsum; 7LGX; -. DR PDBsum; 7LKL; -. DR PDBsum; 7LPF; -. DR PDBsum; 7LT4; -. DR PDBsum; 7LTP; -. DR PDBsum; 7LUT; -. DR PDBsum; 7LV5; -. DR PDBsum; 7LVX; -. DR PDBsum; 7LX1; -. DR PDBsum; 7LY8; -. DR PDBsum; 7M2L; -. DR PDBsum; 7M3S; -. DR PDBsum; 7ME8; -. DR PDBsum; 7MT4; -. DR PDBsum; 7MT5; -. DR PDBsum; 7MT6; -. DR PDBsum; 8B03; -. DR PDBsum; 8B05; -. DR PDBsum; 8B06; -. DR PDBsum; 8B08; -. DR AlphaFoldDB; P0A2K1; -. DR SMR; P0A2K1; -. DR DIP; DIP-35707N; -. DR IntAct; P0A2K1; 1. DR MINT; P0A2K1; -. DR STRING; 99287.STM1726; -. DR DrugBank; DB07748; 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE. DR DrugBank; DB07732; 2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE. DR DrugBank; DB07745; 2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE. DR DrugBank; DB07894; 4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID. DR DrugBank; DB07925; 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID. DR DrugBank; DB07890; 4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID. DR DrugBank; DB07773; 5-FLUOROINDOLE PROPANOL PHOSPHATE. DR DrugBank; DB04143; Indole-3-Glycerol Phosphate. DR DrugBank; DB03171; Indole-3-Propanol Phosphate. DR DrugBank; DB07951; N-(indole-3-acetyl)-L-aspartic acid. DR DrugBank; DB07952; N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID. DR DrugBank; DB07953; N-[1H-INDOL-3-YL-ACETYL]VALINE ACID. DR PaxDb; 99287-STM1726; -. DR GeneID; 1253245; -. DR KEGG; stm:STM1726; -. DR PATRIC; fig|99287.12.peg.1822; -. DR HOGENOM; CLU_016734_3_1_6; -. DR OMA; GIFHGMK; -. DR PhylomeDB; P0A2K1; -. DR BioCyc; SENT99287:STM1726-MONOMER; -. DR UniPathway; UPA00035; UER00044. DR EvolutionaryTrace; P0A2K1; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR CDD; cd06446; Trp-synth_B; 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. 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 INIT_MET 1 FT /note="Removed" FT CHAIN 2..397 FT /note="Tryptophan synthase beta chain" FT /id="PRO_0000098994" FT MOD_RES 87 FT /note="N6-(pyridoxal phosphate)lysine" FT CONFLICT 34 FT /note="S -> R (in Ref. 1; CAA24667/AAA27234)" FT /evidence="ECO:0000305" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:6XSY" FT STRAND 12..17 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 22..36 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 39..51 FT /evidence="ECO:0007829|PDB:7LKL" FT TURN 52..54 FT /evidence="ECO:0007829|PDB:2TSY" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:7LKL" FT TURN 64..68 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 69..77 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 87..100 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 105..113 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 114..126 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 136..141 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 143..151 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 155..159 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:2TRS" FT HELIX 166..177 FT /evidence="ECO:0007829|PDB:7LKL" FT TURN 178..183 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 189..191 FT /evidence="ECO:0007829|PDB:1WBJ" FT HELIX 197..203 FT /evidence="ECO:0007829|PDB:7LKL" FT TURN 204..206 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 207..220 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 235..241 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 250..259 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 270..273 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 274..279 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 281..286 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:1A5A" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 311..318 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 321..328 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 329..343 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 349..364 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 370..376 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 378..380 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 381..383 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 384..393 FT /evidence="ECO:0007829|PDB:7LKL" SQ SEQUENCE 397 AA; 42868 MW; 73D210F5C6F2FEBD CRC64; MTTLLNPYFG EFGGMYVPQI LMPALNQLEE AFVSAQKDPE FQAQFADLLK NYAGRPTALT KCQNITAGTR TTLYLKREDL LHGGAHKTNQ VLGQALLAKR MGKSEIIAET GAGQHGVASA LASALLGLKC RIYMGAKDVE RQSPNVFRMR LMGAEVIPVH SGSATLKDAC NEALRDWSGS YETAHYMLGT AAGPHPYPTI VREFQRMIGE ETKAQILDKE GRLPDAVIAC VGGGSNAIGM FADFINDTSV GLIGVEPGGH GIETGEHGAP LKHGRVGIYF GMKAPMMQTA DGQIEESYSI SAGLDFPSVG PQHAYLNSIG RADYVSITDD EALEAFKTLC RHEGIIPALE SSHALAHALK MMREQPEKEQ LLVVNLSGRG DKDIFTVHDI LKARGEI //