ID   TRPA_YERPS              Reviewed;         268 AA.
AC   Q66AK5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=YPTB2125;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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; BX936398; CAH21363.1; -; Genomic_DNA.
DR   RefSeq; WP_011192442.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66AK5; -.
DR   SMR; Q66AK5; -.
DR   EnsemblBacteria; CAH21363; CAH21363; YPTB2125.
DR   GeneID; 66841441; -.
DR   KEGG; ypo:BZ17_337; -.
DR   KEGG; yps:YPTB2125; -.
DR   PATRIC; fig|273123.14.peg.357; -.
DR   OMA; LVMTYWN; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001011; Chromosome.
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   Tryptophan biosynthesis.
FT   CHAIN           1..268
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098881"
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   268 AA;  28593 MW;  D46B5EA3EFF92332 CRC64;
     MERYQQLFKQ LAAKKEGAFV PFVQLGDPSP AMSLNIIDTL IAAGADALEL GIPFSDPLAD
     GPTIQNAALR AFAAGVTPAI CFEILAEIRQ KHPTIPIGLL MYANLVFHNG IDHFYQRCAE
     VGVDSVLIAD VPFEESAPFR AAALRHGIAP IFICPPNADD DLLREIASHG RGYTYLLSRA
     GVTGAENHGQ LPLNHLVDKL REYNAAPALQ GFGISEPAQV KASLAAGAAG AISGSAIVKI
     IEKNVAQPVE MLVQLTRFVT EMKAATRS