ID   A0A0C7N1T4_9SACH        Unreviewed;       709 AA.
AC   A0A0C7N1T4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Tryptophan synthase {ECO:0000256|ARBA:ARBA00018724, ECO:0000256|RuleBase:RU003663};
DE            EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043, ECO:0000256|RuleBase:RU003663};
GN   ORFNames=LALA0_S01e12310g {ECO:0000313|EMBL:CEP60499.1};
OS   Lachancea lanzarotensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP60499.1, ECO:0000313|Proteomes:UP000054304};
RN   [1] {ECO:0000313|EMBL:CEP60499.1, ECO:0000313|Proteomes:UP000054304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP60499.1,
RC   ECO:0000313|Proteomes:UP000054304};
RA   Neuveglise Cecile;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU003663};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003663};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC       ECO:0000256|RuleBase:RU003663}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the TrpB family.
CC       {ECO:0000256|ARBA:ARBA00005761}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TrpA family.
CC       {ECO:0000256|ARBA:ARBA00006095}.
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DR   EMBL; LN736360; CEP60499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C7N1T4; -.
DR   STRING; 1245769.A0A0C7N1T4; -.
DR   HOGENOM; CLU_016734_2_1_1; -.
DR   OrthoDB; 9569at2759; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000054304; Unassembled WGS sequence.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00131; Trp_synth_alpha; 1.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR018204; Trp_synthase_alpha_AS.
DR   InterPro; IPR002028; Trp_synthase_suA.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00262; trpA; 1.
DR   NCBIfam; TIGR00263; trpB; 1.
DR   PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR   PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00290; Trp_syntA; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU003663};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU003663};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003663};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003663};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054304};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|RuleBase:RU003663}.
FT   DOMAIN          350..675
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   709 AA;  76688 MW;  5FA6862C3300C6FA CRC64;
     MAELLKQTFA NAKAEGRNAL VTFMTAGYPR VEDTIPMLKG FQDGGVDVIE LGMPFSDPIA
     DGPTIQYANT VALRNGVNMV QTLDMVRQAR AEGVTVPIIL MGYYNPIMNF GEEKFIEEAA
     KAGASGFIIV DLPPEEALKL RDLVNYNGLS LIPLVAPSTT DHRLELLSEI ATSFIYVVSR
     MGTTGAQISV SEDVTALVDH VRKFTKDIPL AVGFGVSTRE HFKTVGAVSD GVVIGSQIIK
     LIEECKDNER YEVVKTYVEE ILGGQKHAVL STEEFKQLQT KSIAEGKTRK AAVTNFNEEH
     KFLANFGDFG GQYVPEALHA CLRELEQGFE SAVADPIFWQ QFRDMYSYIG RPSSLHKAER
     LSEHCGGAQI WLKREDLNHT GSHKINNALA QVLIAKRLGK SKIIAETGAG QHGVATATAC
     AKFGLECTVF MGAEDVRRQA LNVFRMRILG ANVVAVTNGT KTLRDATSEA FRFWVSNLKT
     THYVVGSAIG PHPYPTLVRT FQSVIGNETK EQFAKLNDGK LPDAVVACVG GGSNSTGMFS
     PFEHDLSVKL LGVEAGGDGV DTKFHSATLT AGRPGVFHGV KTYVLQDSDG QVHDTHSVSA
     GLDYPGVGPE LASWKASGRA SFIAATDAQA LQGFKILSQL EGIIPALESS HAVYGAIELA
     KTMDKSQHLI INVSGRGDKD VQSVAEVLPK LGPQIGWDLR FEEDPSKSA
//