ID   TRPA_BUCDN              Reviewed;         270 AA.
AC   O68429;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-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};
OS   Buchnera aphidicola subsp. Diuraphis noxia.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9625791; DOI=10.1007/s002849900337;
RA   Baumann L., Baumann P., Moran N.A.;
RT   "The endosymbiont (Buchnera) of the aphid Diuraphis noxia contains all the
RT   genes of the tryptophan biosynthetic pathway.";
RL   Curr. Microbiol. 37:58-59(1998).
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; AF038565; AAC27736.1; -; Genomic_DNA.
DR   RefSeq; WP_075433312.1; NZ_CP013259.1.
DR   AlphaFoldDB; O68429; -.
DR   SMR; O68429; -.
DR   STRING; 118101.ATN01_01375; -.
DR   OrthoDB; 912786at2; -.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..270
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098757"
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   270 AA;  30442 MW;  D8D3E73C4CD81CCD CRC64;
     MNRYENIFDR LSQRKEGCFV PFVVLGDPSL DTSLKIINIL IQNGADALEL GIPFSDPLAD
     GKTIQKANLR ALSQKNNIFQ YFKEIKNLRK KHTQIPIGLL IYANLVYNQG LDNFYLKCRK
     SGVDSVLIAD VPIEESEIFY TTANKYKISS IFICPPNADD DLLYRISLYA KGYIYVLSRP
     GVTGIENQNF FVSGDFIKKI KKYNSVPLLQ GFGISNSIQV KQAISSGLSG VICGSAIINI
     IEKYLYEEDI MMTKIQEFVK HLKKSTKLIA