ID   TRPC_BUCDN              Reviewed;         453 AA.
AC   O68427;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 85.
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. Diuraphis noxia.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9625791; DOI=10.1007/s002849900337;
RA   Baumann L., Baumann P., Moran N.A.;
RT   "The endosymbiont (Buchnera) of the aphid Diuraphis noxia contains all the
RT   genes of the tryptophan biosynthetic pathway.";
RL   Curr. Microbiol. 37:58-59(1998).
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; AF038565; AAC27734.1; -; Genomic_DNA.
DR   AlphaFoldDB; O68427; -.
DR   SMR; O68427; -.
DR   STRING; 118101.ATN01_01385; -.
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..453
FT                   /note="Tryptophan biosynthesis protein TrpCF"
FT                   /id="PRO_0000154274"
FT   REGION          1..257
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          258..453
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ   SEQUENCE   453 AA;  52108 MW;  4ED27374695024A5 CRC64;
     MKETILEKIV KNKYEWIKFR KKKQPLITFK NHINTKTRNF YNSLKEKNPV FILECKKKSP
     SLGIIKKNFN LIDIAKIYNK YASAISVLTD EKYFDGKLEF INIVRERVSQ PILCKDFFID
     PFQIYLARYY NADAILLMLS ILDDFQYQKL SKIAKELNMG ILTEVNNTSE LKRAIKLNAN
     IIGINNRNLH DLSINLNRTR ILSSLIPKNI IIISESGITK YKQIRYLSQF VNGFLIGSHL
     MSEKQLEIGV RSLILGENKI CGLTRSCDIE IAEKYGAVYG GLIFAPSSLR KISKNTAKKI
     IFNNTLRNVG VFQNENIEIV KNIAEELNLY AVQLHGQEDQ KYVKKLRQTL SINIQIWKAF
     SIDSKIPDLN WDHIHKYVLD SQFGGSNKCF NWSILKHQIL ENVILAGGIN SNNCIKASKL
     NCSGLDLNSG IEVSPGIKDH KKIKSVFQKL RYY