ID L0EE63_THECK Unreviewed; 268 AA.
AC L0EE63;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000256|HAMAP-Rule:MF_00131};
GN OrderedLocusNames=Theco_1840 {ECO:0000313|EMBL:AGA57971.1};
OS Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA57971.1, ECO:0000313|Proteomes:UP000010795};
RN [1] {ECO:0000313|Proteomes:UP000010795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18247 / JCM 13945 / KWC4
RC {ECO:0000313|Proteomes:UP000010795};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA Woyke T.;
RT "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC {ECO:0000256|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:0000256|ARBA:ARBA00000003, ECO:0000256|HAMAP-
CC Rule:MF_00131};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC ECO:0000256|HAMAP-Rule:MF_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00131}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000256|HAMAP-
CC Rule:MF_00131, ECO:0000256|RuleBase:RU003662}.
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DR EMBL; CP003255; AGA57971.1; -; Genomic_DNA.
DR RefSeq; WP_015254722.1; NC_019897.1.
DR AlphaFoldDB; L0EE63; -.
DR STRING; 717605.Theco_1840; -.
DR KEGG; tco:Theco_1840; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_9; -.
DR OrthoDB; 9804578at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000010795; 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; 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00131};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00131};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00131};
KW Reference proteome {ECO:0000313|Proteomes:UP000010795};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00131}.
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 268 AA; 29226 MW; 254123693DCAFBCC CRC64;
MNRIDATFER LRREGKSALI PFLTIGDPDL AASAELIAAC AAAGADMIEL GVPYSDPLAD
GPVIQRASER ALQNRVTLED VVRTAAEARR LGADIPYILF SYYNPVLQYG LDRFFKLLEE
HDISGLIVPD LPLEEDGELR DRAEAAGIHL IPLVAPTSHE RIARITARAR GFVYCVSSLG
VTGMRSEFHA SIDDFLASVR SASPVPICVG FGISNREQVL RFEGKTDGVI VGSAIVRKIE
EALPLLGDSG KRAEGVRQVE QFIRSLRV
//
