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 01-MAY-2013, entry version 134.
DE RecName: Full=Tryptophan synthase alpha chain;
DE EC=4.2.1.20;
GN Name=trpA; OrderedLocusNames=STM1727;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
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
RT Escherichia 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
RT tryptophan 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.,
RA Waterston R., Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=4571777;
RA Li S.-L., Yanofsky C.;
RT "Amino acid sequence studies with the tryptophan synthetase alpha
RT chain of Salmonella typhimurium.";
RL J. Biol. Chem. 248:1830-1836(1973).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=3053720;
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
RT alpha2beta2 complex with ligands bound to the active sites of the
RT alpha- and beta-subunits reveal ligand-induced conformational
RT 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
RT phosphate, bound to a mutant (alphaD60N) tryptophan synthase
RT alpha2beta2 complex reveals the correct orientation of active site
RT 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.,
RA Anderson K.S., Lolis E.;
RT "Crystallographic studies of phosphonate-based alpha-reaction
RT transition-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-
RT subunit communication in the beta A169L/beta C170W mutant of
RT 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
CC of indoleglycerol phosphate to indole and glyceraldehyde 3-
CC phosphate.
CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-
CC phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O.
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 -!- INTERACTION:
CC P0A2K1:trpB; NbExp=20; IntAct=EBI-1028423, EBI-1028431;
CC -!- SIMILARITY: Belongs to the TrpA family.
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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_003197.1.
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 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 ProteinModelPortal; P00929; -.
DR SMR; P00929; 1-268.
DR DIP; DIP-1033N; -.
DR IntAct; P00929; 1.
DR MINT; MINT-112862; -.
DR STRING; 99287.STM1727; -.
DR PRIDE; P00929; -.
DR EnsemblBacteria; AAL20645; AAL20645; STM1727.
DR GeneID; 1253246; -.
DR KEGG; stm:STM1727; -.
DR PATRIC; 32381967; VBISalEnt20916_1823.
DR HOGENOM; HOG000223814; -.
DR KO; K01695; -.
DR OMA; VFICPPN; -.
DR ProtClustDB; PRK13111; -.
DR UniPathway; UPA00035; UER00044.
DR EvolutionaryTrace; P00929; -.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:HAMAP.
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 Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; RibP_bind_barrel; 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; Complete proteome;
KW Direct protein sequencing; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1 268 Tryptophan synthase alpha chain.
FT /FTId=PRO_0000098839.
FT ACT_SITE 49 49 Proton acceptor.
FT ACT_SITE 60 60 Proton acceptor.
FT HELIX 3 13
FT STRAND 18 24
FT TURN 25 28
FT HELIX 30 42
FT STRAND 46 51
FT STRAND 58 60
FT HELIX 62 73
FT HELIX 78 91
FT STRAND 93 95
FT STRAND 97 101
FT HELIX 103 107
FT HELIX 111 121
FT STRAND 125 128
FT HELIX 133 135
FT HELIX 137 145
FT STRAND 149 151
FT HELIX 160 169
FT STRAND 174 181
FT STRAND 185 187
FT HELIX 194 202
FT STRAND 208 213
FT HELIX 217 225
FT STRAND 229 233
FT HELIX 235 243
FT TURN 244 246
FT HELIX 248 264
FT TURN 265 267
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
//
