ID   TRP_COPC7               Reviewed;         704 AA.
AC   A8NEP3; D6RKG0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Tryptophan synthase;
DE            EC=4.2.1.20;
GN   Name=TRP-1; ORFNames=CC1G_13871;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
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DR   EMBL; AACS02000002; EFI28341.1; -; Genomic_DNA.
DR   RefSeq; XP_002911835.1; XM_002911789.1.
DR   AlphaFoldDB; A8NEP3; -.
DR   SMR; A8NEP3; -.
DR   STRING; 5346.XP_002911835.1; -.
DR   PRIDE; A8NEP3; -.
DR   EnsemblFungi; EFI28341; EFI28341; CC1G_13871.
DR   GeneID; 9379836; -.
DR   KEGG; cci:CC1G_13871; -.
DR   VEuPathDB; FungiDB:CC1G_13871; -.
DR   eggNOG; KOG1395; Eukaryota.
DR   eggNOG; KOG4175; Eukaryota.
DR   HOGENOM; CLU_016734_1_2_1; -.
DR   InParanoid; A8NEP3; -.
DR   OMA; VDTARHS; -.
DR   OrthoDB; 591064at2759; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001861; 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; 3.20.20.70; -; 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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..704
FT                   /note="Tryptophan synthase"
FT                   /id="PRO_0000333268"
FT   REGION          1..292
FT                   /note="Tryptophan synthase alpha chain"
FT   REGION          293..704
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         380
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   704 AA;  75724 MW;  D7006B8FD54B6D9B CRC64;
     MEAIKKVFEQ KKAQDATAFV AFVTAGYPKK EDTVPVLLAL QAGGADIIEL GIPFSDPIAD
     GPVIQEANTV ALKNDIDYPT VLGQIREARQ QGLTAPVLLM GYYNPMLAYG EDKAIQDAAE
     AGANGFIMVD LPPEEAIAFR QKCAASNLSY VPLIAPSTTL KRIQFLASIA DSFIYVVSKM
     GTTGSSANVA VNEELPTILS RIREYTHVPL AVGFGVATRD QFNYVADAGA DGVVIGSRIV
     NAIKAAGDGE VPQFVENYCR EVSGKGEPSR VRSPGAAQRT PSQLTPNAET AKGVENILPA
     RFGQFGGQYV PESLVDALAE LEEAHKSAIE DPAFWEEVRS LYTYSNRPSN LYLAENLTKE
     AGGANIWLKR EDLNHTGSHK INNALGQILL AKRIGKTRII AETGAGQHGV ATATVCAKFG
     LECVIYMGAE DVRRQALNVF RIEMLGGKAW VIPVHSGSCT LKDAVNEAMR DWVTNLSTTH
     YLVGSAIGPH PFPTIVRDFQ KVIGEEIKAQ LKEVRGKLPD VVVACVGGGS NAIGTFYDFI
     PDKSVRLVGV EAGGEGIDGH KHSATLSMGQ PGVLHGVRTY ILQDKAGQII ETHSISAGLD
     YPGVGPEHAW LKDSGRADYV VCTDEDALRG FRMLTQKEGI IPALESSHAI WEGVKIAKSL
     PKDKDIVICL SGRGDKDVEQ ISELLPKWAD KLDWHVSSNA IPSK