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TRPA_CYAM1
ID   TRPA_CYAM1              Reviewed;         243 AA.
AC   O22018;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 112.
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   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Ohta N., Sato N., Ueda K., Kuroiwa T.;
RT   "Analysis of a plastid gene cluster reveals a close relationship between
RT   Cyanidioschyzon and Cyanidium.";
RL   J. Plant Res. 110:235-245(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3377 / 10D;
RX   PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA   Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA   Shin-i T., Kohara Y., Kuroiwa T.;
RT   "Complete sequence and analysis of the plastid genome of the unicellular
RT   red alga Cyanidioschyzon merolae.";
RL   DNA Res. 10:67-77(2003).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
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DR   EMBL; D63675; BAA22814.1; -; Genomic_DNA.
DR   EMBL; AB002583; BAC76101.1; -; Genomic_DNA.
DR   RefSeq; NP_848939.1; NC_004799.1.
DR   AlphaFoldDB; O22018; -.
DR   SMR; O22018; -.
DR   STRING; 45157.CMV006CT; -.
DR   EnsemblPlants; CMV006CT; CMV006CT; CMV006C.
DR   GeneID; 845057; -.
DR   Gramene; CMV006CT; CMV006CT; CMV006C.
DR   KEGG; cme:CymeCp007; -.
DR   eggNOG; KOG4175; Eukaryota.
DR   HOGENOM; CLU_016734_0_2_1; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000007014; Chloroplast.
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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..243
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098905"
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        40
FT                   /note="A -> P (in Ref. 1; BAA22814)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="N -> Y (in Ref. 1; BAA22814)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   243 AA;  27010 MW;  92894FF00CD7F125 CRC64;
     MLIAYLTAGA PDINTTKEAV MKLAKKGADV IEIGVPYSDA LADGAILQKA SKQALMNGFH
     LDHLWNLLSE VNEIEVPLVI LAYYNQIWHY GVEKWVKKLV AHNVKGLIVP DLPYEESKTL
     RQICDRYGLN IIWLISPTTN KTRAQELARA CKDWIYVISR TGVTGLETEF DKQIPKLIGE
     LKKVTKAPIA LGFGISKSEQ VKLVKSWGAD GVIIGSACMQ ILLEKGVDQL SEWISVMKKS
     FCP
 
 
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