ID   TRP_COPCI               Reviewed;         705 AA.
AC   P16578; Q12576;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 3.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Tryptophan synthase;
DE            EC=4.2.1.20;
GN   Name=TRP-1;
OS   Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=5346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H9 X 12890/3;
RX   PubMed=2806911; DOI=10.1016/0378-1119(89)90338-7;
RA   Skrzynia C., Binninger D.M., Alspaugh J.A. II, Pukkila P.J.;
RT   "Molecular characterization of TRP1, a gene coding for tryptophan
RT   synthetase in the basidiomycete Coprinus cinereus.";
RL   Gene 81:73-82(1989).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TrpA family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the TrpB family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP79219.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAP79219.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY326438; AAP79219.1; ALT_SEQ; Genomic_DNA.
DR   PIR; JU0401; JU0401.
DR   AlphaFoldDB; P16578; -.
DR   SMR; P16578; -.
DR   VEuPathDB; FungiDB:CC1G_13871; -.
DR   VEuPathDB; FungiDB:CC2G_005440; -.
DR   UniPathway; UPA00035; UER00044.
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; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00131; Trp_synth_alpha; 1.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001926; PLP-dep.
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; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00290; Trp_syntA; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00262; trpA; 1.
DR   TIGRFAMs; TIGR00263; trpB; 1.
DR   PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Tryptophan biosynthesis.
FT   CHAIN           1..705
FT                   /note="Tryptophan synthase"
FT                   /id="PRO_0000098723"
FT   REGION          1..293
FT                   /note="Tryptophan synthase alpha chain"
FT   REGION          266..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..705
FT                   /note="Tryptophan synthase beta chain"
FT   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         381
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   705 AA;  75937 MW;  711F70FC368B7278 CRC64;
     MEAIKKVFEQ KKAQDATAFV AFVTAGYPKK EDTVPVLLAL QAGGADIIEL GIPFSDPIAD
     GPVIQEANTV ALKNDIDYPT VLGQIREARQ QGLTAPVLLM GYYNPMLAYG EDKAIQDAAE
     AGANGFIMVD LPPEEAIAFR QKCAASNLSY VPLIAPSTTL KRIQFLASIA DSFIYVVSKM
     GTTGSSANVA VNEELPTILS RIREYTHVPL AVEFGVATRD QFNYVADAGA DGVVVIGSRI
     VNAIKAAGEG QVPQFVENYC REVSGKGEPS RVRSPGAAQR TPSQLTPNAE TAKGVENILP
     ARFGQFGGQY VPESLVDALA ELEEAHKSAI EDPAFWEEVR SLYTYSNRPS NLYLAENLTK
     EAGGANIWLK REDLNHTGSH KINNALGQIL LAKRIGKTRI IAETGAGQHG VATATVCAKF
     GLECVIYMGA EDVRRQALKL FRIEMLGGKA WVIPVHSGSC TLKDAVNEAM RDWVTNLSTT
     HYLVGSAIGP HPFPTIVRDF QKVIGEEIKA QLKEVRGKLP DVVVACVGGG SNAIGTFYDF
     IPDKSVRLVG VEAGGEGIDG HKHSATLSMG QPGVLHGVRT YILQDKAGQI IETHSISAGL
     DYPGVGPEHA WLKDSGRADY VVCTDEDALR GFRMLTQKEG IIPALESSHA IWEGVKIAKS
     LPKDKDIVIC LSGRGDKDVE QISELLPKWA DKLDWHVSSN AIPSK