ID   TRPA_THEMA              Reviewed;         239 AA.
AC   P50908;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   02-SEP-2026, entry version 153.
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};
GN   OrderedLocusNames=TM_0137;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
OC   Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7556082; DOI=10.1002/j.1460-2075.1995.tb00118.x;
RA   Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.;
RT   "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the
RT   hyperthermophile Thermotoga maritima.";
RL   EMBO J. 14:4395-4402(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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 + L-tryptophan + H2O;
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; X92729; CAA63392.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD35230.1; -; Genomic_DNA.
DR   PIR; S59050; S59050.
DR   RefSeq; WP_004082732.1; NC_000853.1.
DR   AlphaFoldDB; P50908; -.
DR   SMR; P50908; -.
DR   FunCoup; P50908; 299.
DR   STRING; 243274.TM_0137; -.
DR   PaxDb; 243274-TM_0137; -.
DR   DNASU; 896967; -.
DR   EnsemblBacteria; AAD35230; AAD35230; TM_0137.
DR   KEGG; tma:TM0137; -.
DR   KEGG; tmi:THEMA_04120; -.
DR   KEGG; tmm:Tmari_0135; -.
DR   KEGG; tmw:THMA_0132; -.
DR   eggNOG; COG0159; Bacteria.
DR   InParanoid; P50908; -.
DR   OrthoDB; 9804578at2; -.
DR   BioCyc; MetaCyc:MONOMER-344; -.
DR   SABIO-RK; P50908; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR00262; trpA; 1.
DR   PANTHER; PTHR43406:SF1; TRYPTOPHAN SYNTHASE ALPHA CHAIN, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43406; TRYPTOPHAN SYNTHASE, ALPHA CHAIN; 1.
DR   Pfam; PF00290; Trp_syntA; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 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..239
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098864"
FT   ACT_SITE        34
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   CONFLICT        189
FT                   /note="F -> L (in Ref. 1; CAA63392)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   239 AA;  26759 MW;  F6B06FBCA83294FA CRC64;
     MKGFIAYIPA GFPDLETTRK ILIALNELGI TGVEIGVPFS DPVADGPVIQ LAHSVALRNG
     VTIKKILEML SEISVDYDLY LMSYLNPIVN YPEGKEKLLD ELKKLGVKGL IIPDLPLREV
     KNVDIAYPIV PFVAPNTKDE EIDLINSVQA PFVYYISRYG VTGEREDLPF ADHIKRVKER
     IKLPLFVGFG ISRHEQVKKV WEIADGVIVG SALVRIMEEN PKDEIPRKVV EKVKELLGK
//