ID   TRPA_HALS3              Reviewed;         276 AA.
AC   B0R333;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=OE_1471F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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; AM774415; CAP13143.1; -; Genomic_DNA.
DR   RefSeq; WP_010902182.1; NC_010364.1.
DR   AlphaFoldDB; B0R333; -.
DR   SMR; B0R333; -.
DR   EnsemblBacteria; CAP13143; CAP13143; OE_1471F.
DR   GeneID; 5954429; -.
DR   KEGG; hsl:OE_1471F; -.
DR   HOGENOM; CLU_016734_0_0_2; -.
DR   OMA; LVMTYWN; -.
DR   PhylomeDB; B0R333; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001321; Chromosome.
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..276
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_1000095719"
FT   ACT_SITE        46
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   ACT_SITE        57
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   276 AA;  28448 MW;  4EC0180D57A89CAE CRC64;
     MTRSDLAAAF DDGPALVSYV VAGDPTPAAT AEYIDALVDG GTDVIELGLP FSEPVAEGTT
     IQNAIKRALD AGMTPDAYLD LVARIDADVP VVCMTYYNLL FQYGDRAGPA AFVSAAAEAG
     VSGFVVPDLP VDESGPLREA CRAHGLDLVF VVAPTTTADR RERMLDLTTG FVYVQGRVGT
     TGAREEVSAA TPDALAALQH TDIPKAVGFG VSSGEQAREI TASGADGVIV GSAYVDTVAD
     GVADDDPPSV VADRLRDLAA ELKAGAARGV PEPEHK