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Entry: P00929
LinkDB: P00929
Original site: P00929 
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   19-FEB-2014, entry version 139.
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 + D-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=22; 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   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   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   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; DYPPEEC; -.
DR   OrthoDB; EOG6RVG0K; -.
DR   ProtClustDB; PRK13111; -.
DR   BioCyc; SENT99287:GCTI-1736-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   EvolutionaryTrace; P00929; -.
DR   PRO; PR:P00929; -.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-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; 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; 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
//
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