ID   TRPC_BUCSC              Reviewed;         461 AA.
AC   Q44603;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Tryptophan biosynthesis protein TrpCF;
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=trpC; Synonyms=trpC/F;
OS   Buchnera aphidicola subsp. Schlechtendalia chinensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7742976; DOI=10.1111/j.1365-2583.1995.tb00007.x;
RA   Lai C.-Y., Baumann P., Moran N.A.;
RT   "Genetics of the tryptophan biosynthetic pathway of the prokaryotic
RT   endosymbiont (Buchnera) of the aphid Schlechtendalia chinensis.";
RL   Insect Mol. Biol. 4:47-59(1995).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of
CC       tryptophan biosynthetic pathway. The first reaction is catalyzed by the
CC       isomerase, coded by the TrpF domain; the second reaction is catalyzed
CC       by the synthase, coded by the TrpC domain (By similarity).
CC       {ECO:0000250}.
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; U09185; AAA92795.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q44603; -.
DR   SMR; Q44603; -.
DR   STRING; 118110.XW81_01310; -.
DR   PRIDE; Q44603; -.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00331; IGPS; 1.
DR   CDD; cd00405; PRAI; 1.
DR   Gene3D; 3.20.20.70; -; 2.
DR   HAMAP; MF_00134_B; IGPS_B; 1.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR001240; PRAI_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR22854; PTHR22854; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; SSF51366; 2.
DR   PROSITE; PS00614; IGPS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW   Isomerase; Lyase; Multifunctional enzyme; Tryptophan biosynthesis.
FT   CHAIN           1..461
FT                   /note="Tryptophan biosynthesis protein TrpCF"
FT                   /id="PRO_0000154275"
FT   REGION          1..258
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          259..461
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ   SEQUENCE   461 AA;  52784 MW;  F202C81D6419D68D CRC64;
     MVLENILEKI VKSKINWIKH RKKIQPLSSF QHNITLSDRN FIQALKNIHP ALILEFKKHS
     PSLGILNDFN PEFVAKIYKK YASAISVLTD EKYFHGKFEF IPIIRNIAVQ QPILCKDFFI
     DPYQIYLARY YQADSILLML SILKDNQYRA LEKLAYSLNM AVLTEINNKM ELDRAINLNA
     KIIGINNRNL KNFSISTSNT YKLASKISKN TIVISESGIN SYNQLRKFKN LVQGFLIGSA
     LMSKKDLEHA VHKIITGNNK ICGLTRVEDA RMSKDFGAIY GGFIFCKSSK RYVNLKKAMN
     ITKNVHMKYI GVFCNENIST ISYIIDKIPL YAIQLHGNEN QFYIDCLKKK IPKCVRVWKA
     ISLNGEKKHA NNLFDNVNKH VFDNIHGGSG TPFNWYLLKN YNLKNVILAG GLNIKNCISA
     SDLGCFGLDF NSGIEISPGL KDKKKTFLIF RSLREHKTII H