ID   TRPA_THEKO              Reviewed;         251 AA.
AC   Q9YGA9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=TK0258;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=10628865; DOI=10.1007/s004380051145;
RA   Tang X., Ezaki S., Fujiwara S., Takagi M., Atomi H., Imanaka T.;
RT   "The tryptophan biosynthesis gene cluster trpCDEGFBA from Pyrococcus
RT   kodakaraensis KOD1 is regulated at the transcriptional level and expressed
RT   as a single mRNA.";
RL   Mol. Gen. Genet. 262:815-821(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AB030011; BAA82551.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD84447.1; -; Genomic_DNA.
DR   PIR; T43928; T43928.
DR   RefSeq; WP_011249213.1; NC_006624.1.
DR   AlphaFoldDB; Q9YGA9; -.
DR   SMR; Q9YGA9; -.
DR   IntAct; Q9YGA9; 1.
DR   MINT; Q9YGA9; -.
DR   STRING; 69014.TK0258; -.
DR   EnsemblBacteria; BAD84447; BAD84447; TK0258.
DR   GeneID; 3234424; -.
DR   KEGG; tko:TK0258; -.
DR   PATRIC; fig|69014.16.peg.257; -.
DR   eggNOG; arCOG01086; Archaea.
DR   HOGENOM; CLU_016734_0_2_2; -.
DR   InParanoid; Q9YGA9; -.
DR   OMA; LVMTYWN; -.
DR   OrthoDB; 65368at2157; -.
DR   PhylomeDB; Q9YGA9; -.
DR   BioCyc; MetaCyc:MON-3561; -.
DR   BRENDA; 4.2.1.20; 5246.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..251
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098898"
FT   ACT_SITE        36
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   ACT_SITE        47
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   251 AA;  27747 MW;  2D9F9FECDD2BFF32 CRC64;
     MFEKGSLIPY LTAGDPSVEK TLEFLLAVEE FAGLIELGIP FSDPMADGKT IQESHYRALR
     NGFKLDDTFR ILREFRRHSS TPVILMTYYN PVFRTGVKKF LGEAKASGAD GILVVDLPVS
     HAGEFLDAAK EEGLKTVFLA APNTPDERLR EIDKASTGFV YLISLYGTTG ARDRLPETAF
     EFVRRARKIC NNKLAVGFGV SRREQVEELL KAGADGVVVG SALIELISRS ENPVEELRRK
     VAELSGYSRA L