ID   TRPC_PHYPR              Reviewed;         531 AA.
AC   P24920;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Tryptophan biosynthesis protein TRP1;
DE   Includes:
DE     RecName: Full=Indole-3-glycerol phosphate synthase;
DE              Short=IGPS;
DE              EC=4.1.1.48;
DE   Includes:
DE     RecName: Full=N-(5'-phospho-ribosyl)anthranilate isomerase;
DE              Short=PRAI;
DE              EC=5.3.1.24;
GN   Name=TRP1;
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1756978; DOI=10.1016/0378-1119(91)90603-9;
RA   Karlovsky P., Prell H.H.;
RT   "The TRP1 gene of Phytophthora parasitica encoding indole-3-
RT   glycerolphosphate synthase-N-(5'-phosphoribosyl)anthranilate isomerase:
RT   structure and evolutionary distance from homologous fungal genes.";
RL   Gene 109:161-165(1991).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of
CC       tryptophan biosynthetic pathway.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC         carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC         EC=5.3.1.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC         = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC         Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the TrpF family.
CC       {ECO:0000305}.
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DR   EMBL; M64473; AAA33751.1; -; Genomic_DNA.
DR   AlphaFoldDB; P24920; -.
DR   SMR; P24920; -.
DR   VEuPathDB; FungiDB:PPTG_16326; -.
DR   BRENDA; 5.3.1.24; 4813.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00331; IGPS; 1.
DR   CDD; cd00405; PRAI; 1.
DR   Gene3D; 3.20.20.70; -; 2.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001240; PRAI_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00218; IGPS; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; SSF51366; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW   Isomerase; Lyase; Multifunctional enzyme; Tryptophan biosynthesis.
FT   CHAIN           1..531
FT                   /note="Tryptophan biosynthesis protein TRP1"
FT                   /id="PRO_0000154306"
FT   REGION          1..254
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          255..531
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ   SEQUENCE   531 AA;  57375 MW;  C154137A6A419ED1 CRC64;
     MGNILEEIAA QRRLDVAAAK QVVSTDDLAK KIEHTESVYG PALPVLERLN APAEQVQAYA
     NAGASMISVL TEPKWFKGSL DDMMEAREVV EGMSQRPAIL RKDFIIDVYQ LLEARAYGAD
     CVLLIVTLLS KEQLIELIDA THNLGMCALV EVNSVQELDI ALAAKARLIG VNNRDLRTFK
     VDMNTTARVA DAIRERGLSL GRDGVALFAL SGIRSHTDVV KYEKCGARGI LVGEYLMKSG
     DIATTVKDLL QNVTRHSESG EFALLPPLAK VCGITTVEYA LAALRNGANM IGIIMAEHSP
     RYVEKEEAKA IAKAVREYGE RTGPILSDIL ESHLDDKSDW FHRNVLALRE ACSRAPLVVG
     VFVNKTATEM NAAAEEIGLD LVQLHGDEGF EICKDIKYPT IRALHLPDTA QCDGVDAEAV
     LQQVSEGLAN YILLDTTVKG QQGGTGVAFD WKIAAIFTQA RLPCLMAGGL TPENVVKALS
     VGHPVGVDVS SGVEVKGSPG VKDLDKVAAF LKAVKDHLSV ATLKIDEETE N