ID   TRPA_BURPS              Reviewed;         271 AA.
AC   Q63JM0;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=BPSS1697;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC       indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00131}.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
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DR   EMBL; BX571966; CAH39170.1; -; Genomic_DNA.
DR   RefSeq; WP_004528976.1; NZ_CP009537.1.
DR   RefSeq; YP_111702.1; NC_006351.1.
DR   AlphaFoldDB; Q63JM0; -.
DR   SMR; Q63JM0; -.
DR   STRING; 272560.BPSS1697; -.
DR   EnsemblBacteria; CAH39170; CAH39170; BPSS1697.
DR   KEGG; bps:BPSS1697; -.
DR   PATRIC; fig|272560.51.peg.5109; -.
DR   eggNOG; COG0159; Bacteria.
DR   OMA; LVMTYWN; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000605; Chromosome 2.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..271
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098761"
FT   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   271 AA;  27978 MW;  AC4B9137254195CD CRC64;
     MSRIQNTFAA LAAQGRKGLI PFITAGDPDP AKTVELMHAL AEGGADVIEL GVPFSDPMAD
     GPVIQRSSER ALAKGVTLHS VLDDVKRFRA RDQKTPVVLM GYANPIERMG ADAFAAAARD
     AGVDGVLVVD YPPEESHDFA AKMRAAGIDP IFLLAPTSTD DRIAAVGQVA SGYVYYVSLK
     GVTGAANLDV SSIAGKIPAI KSRVPLPVGV GFGIRDAATA RAVAEVADAV VIGSRLVQLL
     EQAAPERAAA ELAGFVAELR VAIDGAAKPA A