ID   TRPC_ECO57              Reviewed;         453 AA.
AC   Q8X7B7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 3.
DT   27-MAR-2024, entry version 123.
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; OrderedLocusNames=Z2549, ECs1834;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
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; AE005174; AAG56554.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35257.1; -; Genomic_DNA.
DR   PIR; B90858; B90858.
DR   PIR; F85761; F85761.
DR   RefSeq; NP_309861.1; NC_002695.1.
DR   RefSeq; WP_000983857.1; NZ_VOAI01000015.1.
DR   AlphaFoldDB; Q8X7B7; -.
DR   SMR; Q8X7B7; -.
DR   STRING; 155864.Z2549; -.
DR   GeneID; 912854; -.
DR   KEGG; ece:Z2549; -.
DR   KEGG; ecs:ECs_1834; -.
DR   PATRIC; fig|386585.9.peg.1933; -.
DR   eggNOG; COG0134; Bacteria.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_007713_0_0_6; -.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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; Aldolase class I; 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:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 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; Reference proteome;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..453
FT                   /note="Tryptophan biosynthesis protein TrpCF"
FT                   /id="PRO_0000154278"
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;  49433 MW;  7C30E71A58270033 CRC64;
     MMQTVLAKIV ADKAIWVEAR KQQQPLASFQ NEVQPSTRHF YDALQGARTA FILECKKASP
     SKGVICDDFD PARIAAIYKH YASAISVLTD EKYFQGSFDF LPIVSQIAPQ PILCKDFIID
     PYQIYLARYY QADACLLMLS VLDDEQYRQL AAVAHSLKMG VLTEVSNEEE LERAIALGAK
     VVGINNRDLR DLSIDLNRTR ELAPKLGHNV TVISESGINT YAQVRELSHF ADGFLIGSAL
     MAHDDLHAAV RRVLLGENKV CGLTRGQDAK AAYDAGAIYG GLIFVATSPR CVNVEQAQEV
     MAAAPLQYVG VFRNHDIADV LDKAKVLSLV AVQLHGNEDQ LYIDTLREAL PAHVAIWKAL
     SVGETLPARE LQHVDKYVLD NGQGGSGQRF DWSLLNGQSL GNVLLAGGLG ADNCVEAAQT
     GCAGLDFNSA VESQPGIKDA RLLASVFQTL RAY
//