ID TRPA_SALTY Reviewed; 268 AA. AC P00929; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 02-SEP-2026, entry version 198. DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131}; DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131}; GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; GN OrderedLocusNames=STM1727; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 [3] 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 [4] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=4571777; DOI=10.1016/s0021-9258(19)44265-8; RA Li S.-L., Yanofsky C.; RT "Amino acid sequence studies with the tryptophan synthetase alpha chain of RT Salmonella typhimurium."; RL J. Biol. Chem. 248:1830-1836(1973). RN [5] 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 [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). 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 [7] 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 [8] 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 [9] 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 [10] 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). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 17-268. RX PubMed=12460570; DOI=10.1016/s0022-2836(02)01109-9; RA Kulik V., Weyand M., Seidel R., Niks D., Arac D., Dunn M.F., RA Schlichting I.; RT "On the role of alphaThr183 in the allosteric regulation and catalytic RT mechanism of tryptophan synthase."; RL J. Mol. Biol. 324:677-690(2002). CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00131}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC -!- INTERACTION: CC P00929; P0A2K1: trpB; NbExp=24; IntAct=EBI-1028423, EBI-1028431; CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP- CC Rule:MF_00131}. 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; V01376; CAA24666.1; -; Genomic_DNA. DR EMBL; J01810; AAA27235.1; -; Genomic_DNA. DR EMBL; AE006468; AAL20645.1; -; Genomic_DNA. DR PIR; A93837; TSEBAT. DR RefSeq; NP_460686.1; NC_003197.2. DR RefSeq; WP_000443030.1; NC_003197.2. DR PDB; 1A50; X-ray; 2.30 A; A=1-268. DR PDB; 1A5A; X-ray; 1.90 A; A=1-268. DR PDB; 1A5B; X-ray; 2.00 A; A=1-268. DR PDB; 1A5S; X-ray; 2.30 A; A=1-268. DR PDB; 1BEU; X-ray; 1.90 A; A=1-268. DR PDB; 1BKS; X-ray; 2.20 A; A=1-268. DR PDB; 1C29; X-ray; 2.30 A; A=1-268. DR PDB; 1C8V; X-ray; 2.20 A; A=1-268. DR PDB; 1C9D; X-ray; 2.30 A; A=1-268. DR PDB; 1CW2; X-ray; 2.00 A; A=1-268. DR PDB; 1CX9; X-ray; 2.30 A; A=1-268. DR PDB; 1FUY; X-ray; 2.25 A; A=1-268. DR PDB; 1K3U; X-ray; 1.70 A; A=1-268. DR PDB; 1K7E; X-ray; 2.30 A; A=1-268. DR PDB; 1K7F; X-ray; 1.90 A; A=1-268. DR PDB; 1K7X; X-ray; 1.70 A; A=1-268. DR PDB; 1K8X; X-ray; 1.90 A; A=1-268. DR PDB; 1K8Y; X-ray; 1.50 A; A=1-268. DR PDB; 1K8Z; X-ray; 1.70 A; A=1-268. DR PDB; 1KFB; X-ray; 1.90 A; A=1-268. DR PDB; 1KFC; X-ray; 1.50 A; A=1-268. DR PDB; 1KFE; X-ray; 1.75 A; A=1-268. DR PDB; 1KFJ; X-ray; 1.80 A; A=1-268. DR PDB; 1KFK; X-ray; 2.40 A; A=1-268. DR PDB; 1QOP; X-ray; 1.40 A; A=1-268. DR PDB; 1QOQ; X-ray; 1.80 A; A=1-268. DR PDB; 1TJP; X-ray; 1.50 A; A=1-268. DR PDB; 1TTP; X-ray; 2.30 A; A=1-268. DR PDB; 1TTQ; X-ray; 2.00 A; A=1-268. DR PDB; 1UBS; X-ray; 1.90 A; A=1-268. DR PDB; 1WBJ; X-ray; 1.50 A; A=1-268. DR PDB; 2CLE; X-ray; 1.50 A; A=1-268. DR PDB; 2CLF; X-ray; 1.70 A; A=1-268. DR PDB; 2CLH; X-ray; 1.70 A; A=1-268. DR PDB; 2CLI; X-ray; 1.70 A; A=1-268. DR PDB; 2CLK; X-ray; 1.50 A; A=1-268. DR PDB; 2CLL; X-ray; 1.60 A; A=1-268. DR PDB; 2CLM; X-ray; 1.51 A; A=1-268. DR PDB; 2CLO; X-ray; 1.50 A; A=1-268. DR PDB; 2J9X; X-ray; 1.90 A; A=1-268. DR PDB; 2J9Y; X-ray; 1.80 A; A=1-268. DR PDB; 2J9Z; X-ray; 1.80 A; A=1-268. DR PDB; 2RH9; X-ray; 1.70 A; A=1-268. DR PDB; 2RHG; X-ray; 2.00 A; A=1-268. DR PDB; 2TRS; X-ray; 2.04 A; A=1-268. DR PDB; 2TSY; X-ray; 2.50 A; A=1-268. DR PDB; 2TYS; X-ray; 1.90 A; A=1-268. DR PDB; 2WSY; X-ray; 3.05 A; A=1-268. DR PDB; 3CEP; X-ray; 2.10 A; A=1-268. DR PDB; 3PR2; X-ray; 1.85 A; A=2-267. DR PDB; 4HN4; X-ray; 1.64 A; A=1-268. DR PDB; 4HPJ; X-ray; 1.45 A; A=1-268. DR PDB; 4HPX; X-ray; 1.65 A; A=1-268. DR PDB; 4HT3; X-ray; 1.30 A; A=1-268. DR PDB; 4KKX; X-ray; 1.77 A; A=1-268. DR PDB; 4WX2; X-ray; 1.75 A; A=1-268. DR PDB; 4XUG; X-ray; 1.65 A; A=1-268. DR PDB; 4Y6G; X-ray; 1.65 A; A=1-268. DR PDB; 4ZQC; X-ray; 1.54 A; A=1-268. DR PDB; 5BW6; X-ray; 1.82 A; A=1-268. DR PDB; 5CGQ; X-ray; 1.18 A; A=1-268. DR PDB; 6C73; X-ray; 1.65 A; A=1-268. DR PDB; 6D0V; X-ray; 1.64 A; A=1-268. DR PDB; 6DUC; X-ray; 1.79 A; A=1-268. DR PDB; 6DZ4; X-ray; 1.45 A; A=1-268. DR PDB; 6DZO; X-ray; 1.64 A; A=1-268. DR PDB; 6O1H; X-ray; 1.64 A; A=1-268. DR PDB; 6OSO; X-ray; 1.75 A; A=1-268. DR PDB; 6OUY; X-ray; 1.60 A; A=1-268. DR PDB; 6VFD; X-ray; 1.70 A; A=1-268. DR PDB; 6VNT; X-ray; 1.25 A; A=1-268. DR PDB; 6WDU; X-ray; 1.40 A; A=1-268. DR PDB; 6WX3; X-ray; 1.20 A; A=1-268. DR PDB; 6X0C; X-ray; 1.45 A; A=1-268. DR PDB; 6XE3; X-ray; 1.55 A; A=1-268. DR PDB; 6XIN; X-ray; 1.75 A; A=1-268. DR PDB; 6XNC; X-ray; 2.11 A; A=1-268. DR PDB; 6XOY; X-ray; 1.64 A; A=1-268. DR PDB; 6XRH; X-ray; 1.44 A; A=1-268. DR PDB; 6XSY; X-ray; 1.55 A; A=1-268. DR PDB; 6XT0; X-ray; 1.37 A; A=1-268. DR PDB; 7A20; X-ray; 2.50 A; A/B/C/D=1-268. DR PDB; 7JHW; X-ray; 1.65 A; A=1-268. DR PDB; 7JLL; X-ray; 1.55 A; A=1-268. DR PDB; 7JMQ; X-ray; 1.60 A; A=1-268. DR PDB; 7JQW; X-ray; 1.70 A; A=1-268. DR PDB; 7JTT; X-ray; 1.64 A; A=1-268. DR PDB; 7K0B; X-ray; 1.57 A; A=1-268. DR PDB; 7K5A; X-ray; 1.50 A; A=1-268. DR PDB; 7KA1; X-ray; 1.60 A; A=1-268. DR PDB; 7KBN; X-ray; 1.60 A; A=1-268. DR PDB; 7KH6; X-ray; 1.45 A; A=1-268. DR PDB; 7KI7; X-ray; 1.75 A; A=1-268. DR PDB; 7KMC; X-ray; 1.50 A; A=1-268. DR PDB; 7KQ9; X-ray; 1.50 A; A=1-268. DR PDB; 7KQF; X-ray; 1.47 A; A=1-268. DR PDB; 7KU9; X-ray; 1.40 A; A=1-268. DR PDB; 7KWV; X-ray; 1.30 A; A=1-268. DR PDB; 7KXC; X-ray; 1.51 A; A=1-268. DR PDB; 7KYT; X-ray; 1.35 A; A=1-268. DR PDB; 7L03; X-ray; 1.60 A; A=1-268. DR PDB; 7L1H; X-ray; 1.50 A; A=1-268. DR PDB; 7L47; X-ray; 1.55 A; A=1-268. DR PDB; 7L4D; X-ray; 1.60 A; A=1-268. DR PDB; 7L5H; X-ray; 1.80 A; A=1-268. DR PDB; 7LEV; X-ray; 1.70 A; A=1-268. DR PDB; 7LGX; X-ray; 1.80 A; A=1-268. DR PDB; 7LKL; X-ray; 1.05 A; A=1-268. DR PDB; 7LPF; X-ray; 1.10 A; A=1-268. DR PDB; 7LT4; X-ray; 1.80 A; A=1-268. DR PDB; 7LTP; X-ray; 1.47 A; A=1-268. DR PDB; 7LUT; X-ray; 1.60 A; A=1-268. DR PDB; 7LV5; X-ray; 1.60 A; A=1-268. DR PDB; 7LVX; X-ray; 1.55 A; A=1-268. DR PDB; 7LX1; X-ray; 1.61 A; A=1-268. DR PDB; 7LY8; X-ray; 1.55 A; A=1-268. DR PDB; 7M2L; X-ray; 1.60 A; A=1-268. DR PDB; 7M3S; X-ray; 1.55 A; A=1-268. DR PDB; 7ME8; X-ray; 1.60 A; A=1-268. DR PDB; 7MT4; X-ray; 1.40 A; A=1-268. DR PDB; 7MT5; X-ray; 1.50 A; A=1-268. DR PDB; 7MT6; X-ray; 1.70 A; A=1-268. DR PDB; 8B03; X-ray; 2.22 A; A=1-268. DR PDB; 8B05; X-ray; 2.10 A; A=1-268. DR PDB; 8B06; X-ray; 2.49 A; A=1-268. DR PDB; 8B08; X-ray; 2.50 A; A=1-268. DR PDB; 8EYP; Other; 1.80 A; A=1-268. DR PDB; 8EYS; X-ray; 2.20 A; A=1-268. DR PDB; 8EZC; X-ray; 1.60 A; A=1-268. DR PDB; 8RSX; X-ray; 2.00 A; A=1-268. DR PDB; 8RSY; X-ray; 2.11 A; A=1-268. DR PDB; 8RSZ; X-ray; 2.20 A; A=1-268. DR AlphaFoldDB; P00929; -. DR MDposit; P00929; -. DR MDRepo; P00929; -. DR SMR; P00929; -. DR DIP; DIP-1033N; -. DR IntAct; P00929; 1. DR MINT; P00929; -. DR STRING; 99287.STM1727; -. 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-STM1727; -. DR GeneID; 1253246; -. DR KEGG; stm:STM1727; -. DR PATRIC; fig|99287.12.peg.1823; -. DR HOGENOM; CLU_016734_0_4_6; -. DR OMA; LVMTYWN; -. DR PhylomeDB; P00929; -. DR BioCyc; SENT99287:STM1727-MONOMER; -. DR BRENDA; 4.2.1.20; 5542. DR UniPathway; UPA00035; UER00044. DR EvolutionaryTrace; P00929; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule. DR CDD; cd04724; Tryptophan_synthase_alpha; 1. DR FunFam; 3.20.20.70:FF:000037; Tryptophan synthase alpha chain; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00131; Trp_synth_alpha; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR InterPro; IPR018204; Trp_synthase_alpha_AS. DR InterPro; IPR002028; Trp_synthase_suA. DR NCBIfam; TIGR00262; trpA; 1. DR PANTHER; PTHR43406:SF1; TRYPTOPHAN SYNTHASE ALPHA CHAIN, CHLOROPLASTIC; 1. DR PANTHER; PTHR43406; TRYPTOPHAN SYNTHASE, ALPHA CHAIN; 1. DR Pfam; PF00290; Trp_syntA; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1. DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1. 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; 6OSO; -. DR PDBsum; 6OUY; -. 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 PDBsum; 8EYP; -. DR PDBsum; 8EYS; -. DR PDBsum; 8EZC; -. DR PDBsum; 8RSX; -. DR PDBsum; 8RSY; -. DR PDBsum; 8RSZ; -. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Direct protein sequencing; Lyase; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1..268 FT /note="Tryptophan synthase alpha chain" FT /id="PRO_0000098839" FT ACT_SITE 49 FT /note="Proton acceptor" FT ACT_SITE 60 FT /note="Proton acceptor" FT HELIX 3..13 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 18..24 FT /evidence="ECO:0007829|PDB:7LKL" FT TURN 25..28 FT /evidence="ECO:0007829|PDB:1TTP" FT HELIX 30..42 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 46..51 FT /evidence="ECO:0007829|PDB:7LKL" FT TURN 57..59 FT /evidence="ECO:0007829|PDB:6OUY" FT HELIX 62..73 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 78..91 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 103..107 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 111..121 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 137..145 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:7LPF" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:3PR2" FT HELIX 160..169 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 174..177 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:7KWV" FT HELIX 190..193 FT /evidence="ECO:0007829|PDB:5CGQ" FT HELIX 194..202 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 208..213 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 217..225 FT /evidence="ECO:0007829|PDB:7LKL" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 235..243 FT /evidence="ECO:0007829|PDB:7LKL" FT TURN 244..246 FT /evidence="ECO:0007829|PDB:7LKL" FT HELIX 248..264 FT /evidence="ECO:0007829|PDB:7LKL" FT TURN 265..267 FT /evidence="ECO:0007829|PDB:6C73" SQ SEQUENCE 268 AA; 28671 MW; F409BF1A931581B5 CRC64; MERYENLFAQ LNDRREGAFV PFVTLGDPGI EQSLKIIDTL IDAGADALEL GVPFSDPLAD GPTIQNANLR AFAAGVTPAQ CFEMLALIRE KHPTIPIGLL MYANLVFNNG IDAFYARCEQ VGVDSVLVAD VPVEESAPFR QAALRHNIAP IFICPPNADD DLLRQVASYG RGYTYLLSRS GVTGAENRGA LPLHHLIEKL KEYHAAPALQ GFGISSPEQV SAAVRAGAAG AISGSAIVKI IEKNLASPKQ MLAELRSFVS AMKAASRA //