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Database: UniProt/SWISS-PROT
Entry: TRPA_BURM9
LinkDB: TRPA_BURM9
Original site: TRPA_BURM9 
ID   TRPA_BURM9              Reviewed;         271 AA.
AC   A2S138; A2S137;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   01-MAY-2013, entry version 49.
DE   RecName: Full=Tryptophan synthase alpha chain;
DE            EC=4.2.1.20;
GN   Name=trpA; OrderedLocusNames=BMA10229_1859;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE REVISION.
RA   Brinkac L.M., Harkins D.M., Shrivastava S., Durkin A.S., Sutton G.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
CC       of indoleglycerol phosphate to indole and glyceraldehyde 3-
CC       phosphate (By similarity).
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 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TrpA family.
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DR   EMBL; CP000545; ABN00188.2; -; Genomic_DNA.
DR   RefSeq; YP_001025657.1; NC_008835.1.
DR   ProteinModelPortal; A2S138; -.
DR   STRING; 412022.BMA10229_1860; -.
DR   EnsemblBacteria; ABN00188; ABN00188; BMA10229_1859.
DR   GeneID; 4790383; -.
DR   KEGG; bml:BMA10229_1860; -.
DR   PATRIC; 19130169; VBIBurMal46188_1814.
DR   eggNOG; COG0159; -.
DR   HOGENOM; HOG000161821; -.
DR   KO; K01695; -.
DR   OMA; VFICPPN; -.
DR   ProtClustDB; CLSK897166; -.
DR   BioCyc; BMAL412022:GJI8-5266-MONOMER; -.
DR   BioCyc; BMAL412022:GJI8-5267-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Tryptophan biosynthesis.
FT   CHAIN         1    271       Tryptophan synthase alpha chain.
FT                                /FTId=PRO_1000018176.
FT   ACT_SITE     49     49       Proton acceptor (By similarity).
FT   ACT_SITE     60     60       Proton acceptor (By similarity).
SQ   SEQUENCE   271 AA;  27978 MW;  AC4B83AA542695CD 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
     EQAVPERAAA ELAGFVAELR AAIDGAAKPA A
//
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