ID   TRPA_PYRAB              Reviewed;         248 AA.
AC   Q9V1G9; G8ZGG2;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 119.
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=PYRAB04580;
GN   ORFNames=PAB2049;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
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DR   EMBL; AJ248284; CAB49380.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69841.1; -; Genomic_DNA.
DR   PIR; E75162; E75162.
DR   RefSeq; WP_010867582.1; NC_000868.1.
DR   AlphaFoldDB; Q9V1G9; -.
DR   SMR; Q9V1G9; -.
DR   STRING; 272844.PAB2049; -.
DR   PRIDE; Q9V1G9; -.
DR   EnsemblBacteria; CAB49380; CAB49380; PAB2049.
DR   GeneID; 1495354; -.
DR   KEGG; pab:PAB2049; -.
DR   PATRIC; fig|272844.11.peg.485; -.
DR   eggNOG; arCOG01086; Archaea.
DR   HOGENOM; CLU_016734_0_2_2; -.
DR   OMA; LVMTYWN; -.
DR   OrthoDB; 65368at2157; -.
DR   PhylomeDB; Q9V1G9; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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..248
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098896"
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   248 AA;  27288 MW;  400E27D2E17F7440 CRC64;
     MFRDGSLIPY LTAGDPSAKA TLRFLLAIEE YSGAIELGIP FSDPIADGKT IQQSHFRALK
     GGFKLEHAFN IVREFRKHSD VPIVLMTYYN PVFRVGLREF IGKAKDSGVD GMLIVDLPVM
     HASEFLEVAR EEGIKTVFLA APNTPDERLK EIDKASTGFV YLISLYGTTG ARDKIPETAF
     NLLKRAKRIC KNKVAVGFGV SKREHVEMLL NAGANGVVVG SALINIIAEH GENAEEKLRE
     KVRELAGL