ID   TRPA_LEGPA              Reviewed;         272 AA.
AC   Q5X5Q1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=lpp1269;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(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; CR628336; CAH12420.1; -; Genomic_DNA.
DR   RefSeq; WP_011213616.1; NC_006368.1.
DR   PDB; 5KMY; X-ray; 1.91 A; A=1-272.
DR   PDBsum; 5KMY; -.
DR   AlphaFoldDB; Q5X5Q1; -.
DR   SMR; Q5X5Q1; -.
DR   KEGG; lpp:lpp1269; -.
DR   LegioList; lpp1269; -.
DR   HOGENOM; CLU_016734_0_0_6; -.
DR   OMA; LVMTYWN; -.
DR   UniPathway; UPA00035; UER00044.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Lyase; Tryptophan biosynthesis.
FT   CHAIN           1..272
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098796"
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"
FT   HELIX           3..13
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   STRAND          18..24
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           33..42
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           62..73
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           78..89
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           103..109
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           111..121
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           137..146
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           160..167
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           190..201
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   STRAND          208..210
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           217..224
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   STRAND          227..232
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           234..245
FT                   /evidence="ECO:0007829|PDB:5KMY"
FT   HELIX           250..266
FT                   /evidence="ECO:0007829|PDB:5KMY"
SQ   SEQUENCE   272 AA;  29892 MW;  C4F797483FBE1A13 CRC64;
     MNRIDKTLEK LKANRKKMLS PYITAGDPYP ELTVSLMHQL VKSGADVLEL GIPFSDPMAE
     GPVIQRAMER ALAHSIHCDD VLNMVRQFRK TDTETPVILM GYLNPIEQYG YDLFAQQAVE
     AGADGTILVD LPPEEADGVS RVWQKHGLYS IYLCSPTTSA ERMNFINQHA NGYLYYVSLK
     GVTGSDALKL PELKAQYLQR KAQSKLPLMV GFGIKTPEMA AQVAEFADGV IVGAALINEI
     IEAYEAKKDP LQASGALLSS MRQAIDNIGS MV