TRPA_SALTY
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 03-AUG-2022, entry version 185.
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}; OrderedLocusNames=STM1727;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 + 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 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; 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; 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; 7LGX; X-ray; 1.80 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 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; 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; 7L1H; -.
DR PDBsum; 7L47; -.
DR PDBsum; 7L4D; -.
DR PDBsum; 7L5H; -.
DR PDBsum; 7LGX; -.
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 AlphaFoldDB; 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; P00929; -.
DR EnsemblBacteria; AAL20645; AAL20645; 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-MON; -.
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; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
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:5CGQ"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:5CGQ"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1TTP"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:5CGQ"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6OUY"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6VNT"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6VNT"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:5CGQ"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 248..265
FT /evidence="ECO:0007829|PDB:5CGQ"
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
