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Database: UniProt
Entry: B6SCD2_LAMGA
LinkDB: B6SCD2_LAMGA
Original site: B6SCD2_LAMGA 
ID   B6SCD2_LAMGA            Unreviewed;       309 AA.
AC   B6SCD2;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE            EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
OS   Lamium galeobdolon (Yellow archangel) (Galeopsis galeobdolon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Lamioideae; Lamieae; Lamium.
OX   NCBI_TaxID=53161 {ECO:0000313|EMBL:ACJ02773.1};
RN   [1] {ECO:0000313|EMBL:ACJ02773.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18929374; DOI=10.1016/j.phytochem.2008.08.023;
RA   Schullehner K., Dick R., Vitzthum F., Schwab W., Brandt W., Frey M.,
RA   Gierl A.;
RT   "Benzoxazinoid biosynthesis in dicot plants.";
RL   Phytochemistry 69:2668-2677(2008).
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};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|ARBA:ARBA00011270}.
CC   -!- SIMILARITY: Belongs to the TrpA family.
CC       {ECO:0000256|RuleBase:RU003662}.
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DR   EMBL; EU747716; ACJ02773.1; -; mRNA.
DR   AlphaFoldDB; B6SCD2; -.
DR   UniPathway; UPA00035; UER00044.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ACJ02773.1};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
SQ   SEQUENCE   309 AA;  33152 MW;  C406D95766F5716E CRC64;
     MAANSLKSIC FPQLKTTNQS ISQRSSSRVS LCYKPPMATL QTATKAGISE TFSRLKQQGK
     VALIPYITAG DPDLSTTAEA LKVLDSCGSD IIELGVPYSD PLADGPVIQA AATRSLSRGA
     DFDKIIGMLK EVIPQLSCPV GLFTYYNPIL KRGVEEFMTT LKDTGINGLI VPDVPLEETE
     MLRKEATKNN IELVLLTTPT TPSDRMKEIV EAAEGFIYLV STVGVTGTRT SVSDKVQSLL
     HEIKGETNKA VAVGFGISKP EQVKQVAEWG ADGVIVGSAM VKILGEAKTP EEGLKELEKF
     TKTLKSALV
//
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