TRPB_SALTY
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 03-AUG-2022, entry version 126.
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; Proteobacteria; 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}.
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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 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 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; P0A2K1; -.
DR EnsemblBacteria; AAL20644; AAL20644; STM1726.
DR GeneID; 1253245; -.
DR KEGG; stm:STM1726; -.
DR PATRIC; fig|99287.12.peg.1822; -.
DR HOGENOM; CLU_016734_3_1_6; -.
DR OMA; HGMKSYF; -.
DR PhylomeDB; P0A2K1; -.
DR BioCyc; SENT99287:STM1726-MON; -.
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; IPR001926; PLP-dep.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00263; trpB; 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:5CGQ"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:5CGQ"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2TSY"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5CGQ"
FT TURN 63..68
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2TRS"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:5CGQ"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1WBJ"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1A5A"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 329..343
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:5CGQ"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:6VNT"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:5CGQ"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:5CGQ"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:7MT4"
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
