ID   TRPA_KLEAE              Reviewed;         269 AA.
AC   P00930;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   25-MAY-2022, entry version 107.
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};
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6262736; DOI=10.1093/nar/9.7.1743;
RA   Nichols B.P., Blumenberg M., Yanofsky C.;
RT   "Comparison of the nucleoside sequence of trpA and sequences immediately
RT   beyond the trp operon of Klebsiella aerogenes. Salmonella typhimurium and
RT   Escherichia coli.";
RL   Nucleic Acids Res. 9:1743-1755(1981).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=4571778; DOI=10.1016/s0021-9258(19)44266-x;
RA   Li S.-L., Yanofsky C.;
RT   "Amino acid sequence studies with the tryptophan synthetase alpha chain of
RT   Aerobacter aerogenes.";
RL   J. Biol. Chem. 248:1837-1843(1973).
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.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
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DR   EMBL; V00630; CAA23902.1; -; Genomic_DNA.
DR   EMBL; J01738; AAA25145.1; -; Genomic_DNA.
DR   RefSeq; WP_002901728.1; NZ_LR134254.1.
DR   AlphaFoldDB; P00930; -.
DR   SMR; P00930; -.
DR   STRING; 548.EAG7_01141; -.
DR   GeneID; 56939279; -.
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   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Direct protein sequencing; Lyase; Tryptophan biosynthesis.
FT   CHAIN           1..269
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098792"
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   CONFLICT        2
FT                   /note="E -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        13
FT                   /note="N -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="Q -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24
FT                   /note="T -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="P -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="D -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="A -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="K -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="L -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   269 AA;  28544 MW;  844BA0C3FC361647 CRC64;
     MERYETLFAQ LKNRQEGAFV PFVTLGDPGP EQSLKIIDAL IEGGADALEL GIPFSDPLAD
     GPTIQGAALR AFAAGVTPAQ CFEMLAAIRQ KHPTIPIGLL MYANLVFSPG IDAFYAQCAR
     VGVDSVLVAD VPVEESAPFR QAAMRHNIAP IFICPPNADD DLLRQIASYG RGYTYLLSRA
     GVTGAENRAA LPLHHLVEKL AEYHAAPPLQ GFGISAPEQV SAAIDAGAAG AISGSAIVKI
     IERHLDEPQT MLDELKAFVQ SLKAATKTA