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Database: UniProt
Entry: S8BZC7_9LAMI
LinkDB: S8BZC7_9LAMI
Original site: S8BZC7_9LAMI 
ID   S8BZC7_9LAMI            Unreviewed;       277 AA.
AC   S8BZC7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE            EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
DE   Flags: Fragment;
GN   ORFNames=M569_15021 {ECO:0000313|EMBL:EPS59784.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS59784.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS59784.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPS59784.1}.
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DR   EMBL; AUSU01008081; EPS59784.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8BZC7; -.
DR   OrthoDB; 447892at2759; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EPS59784.1"
FT   NON_TER         277
FT                   /evidence="ECO:0000313|EMBL:EPS59784.1"
SQ   SEQUENCE   277 AA;  29641 MW;  CB765438858BD351 CRC64;
     PMAALPAAGI SETFSRLKQQ GKVALIPYIT AGDPDLKTTA EALKTLSNSG ADIIELGVPY
     SDPLADGPVI QAAATRALSR GTNFNKIAAM LKQTIPHLSC PIALFSYYNP ILKRGVESFM
     TALREIGIHG TSRVDCSSGL VVPDIPFEET EILRKEARNN NIELVLLTTP TTPLARMRDI
     VEASQGFVYL VSSVGVTGVR ASVSERVKSL LNEIKRETSK PVAVGFGISK PDHVKQIVEW
     GADGVIVGSA MVKLLGEAKS AEEGLKELEI FTRSLKA
//
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