ID   TRPC_BUCBP              Reviewed;         469 AA.
AC   P59459;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=bbp_259;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26986.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59459; -.
DR   SMR; P59459; -.
DR   STRING; 224915.bbp_259; -.
DR   KEGG; bab:bbp_259; -.
DR   eggNOG; COG0134; Bacteria.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_007713_1_2_6; -.
DR   OrthoDB; 9804217at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000000601; 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..469
FT                   /note="Tryptophan biosynthesis protein TrpCF"
FT                   /id="PRO_0000154273"
FT   REGION          1..257
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          258..469
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ   SEQUENCE   469 AA;  54239 MW;  089802BE9F178FD9 CRC64;
     MNSILKEIIN DKLMWVKYHK KKQPLFTFQN KIVRSNYNFK NSLKSIHPSY ILEIKKASPS
     LGIINNKLDL KKISLIYKKY ASSISILTDE KYFHGNFEFI PIVRKIAHRQ PILCKDFFID
     PYQIYLARYY QADAILLMLS ILNDNQYVFL RNIAEMLNMD VLTEIENKKE LTRAINLKSK
     IIGINNRNLN NLSIDIQKTK VLAPLIPKKI IIISESGIQN YNQIRQLKPF VQGFLIGSNL
     MRKKNLEEAV CKMILGNNKI CGLTQSSDVK IIKEYGIVYG GLIFCKFSPR YINCNNAYSI
     INNVSLKYIG VFCNENLKRV AYIGTKLSLH AVQLHGNEDQ IYINNLKLIL PKHIKIWKSI
     IYLDFLKNQK HLFYNVNKYI IDNKDGGSGK TFNWKYLKNC KLDNVILAGG LDINNCILAT
     DLGCYGYDFN SKLESSPGIK DLKKIVALTY SLRRHTVFNY RNLICLGKK
//