ID   TRPA2_CYACA             Reviewed;         242 AA.
AC   P34793; O22027;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 100.
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   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=8082179; DOI=10.1007/bf00351490;
RA   Ohta N., Sato N., Kawano S., Kuroiwa T.;
RT   "The trpA gene on the plastid genome of Cyanidium caldarium strain RK-1.";
RL   Curr. Genet. 25:357-361(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RK-1;
RA   Ohta N.;
RT   "Analysis of a plastid gene cluster reveals a close relationship between
RT   Cyanidioschyzon and Cyanidium.";
RL   J. Plant Res. 110:235-245(1997).
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC       indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
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DR   EMBL; D17791; BAA04617.1; -; Genomic_DNA.
DR   EMBL; D63676; BAA22823.1; -; Genomic_DNA.
DR   PIR; S41995; S41995.
DR   PIR; T14365; T14365.
DR   AlphaFoldDB; P34793; -.
DR   SMR; P34793; -.
DR   UniPathway; UPA00035; UER00044.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; Chloroplast;
KW   Lyase; Plastid; Tryptophan biosynthesis.
FT   CHAIN           1..242
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098904"
FT   ACT_SITE        32
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   ACT_SITE        43
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   CONFLICT        58
FT                   /note="R -> G (in Ref. 1; BAA04617)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="T -> L (in Ref. 1; BAA04617)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   242 AA;  26894 MW;  35F64D8AB4453470 CRC64;
     MFIAYLTAGA PDLNTTKQAL LNLANDGADV IEIGVPYSDP LADGMILQKA SQQALKNRFR
     LEQLWHLLAE IELPVPVVIL AYYNQIFHYG VEKWVTTLVN LKVKALIVPD LPYEEAAILR
     AACARHHLHM IWLISPTTPK VRAKQLALAC DDWIYLVSRT GVTGVDAHFD NQIPNMIAEL
     KQVTTTPIAL GFGIHQKQQL QLVKSWGADG VIIGTACMQI LLEKGVDQLT EWISAMKKSS
     YP