ID   TRPC_BUCAP              Reviewed;         451 AA.
AC   P42393;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 124.
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; OrderedLocusNames=BUsg_268;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8407819; DOI=10.1128/jb.175.20.6426-6432.1993;
RA   Munson M.A., Baumann P.;
RT   "Molecular cloning and nucleotide sequence of a putative trpDC(F)BA operon
RT   in Buchnera aphidicola (endosymbiont of the aphid Schizaphis graminum).";
RL   J. Bacteriol. 175:6426-6432(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; Z19055; CAA79499.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67826.1; -; Genomic_DNA.
DR   PIR; B49897; B49897.
DR   RefSeq; WP_011053793.1; NC_004061.1.
DR   AlphaFoldDB; P42393; -.
DR   SMR; P42393; -.
DR   STRING; 198804.BUsg_268; -.
DR   EnsemblBacteria; AAM67826; AAM67826; BUsg_268.
DR   KEGG; bas:BUsg_268; -.
DR   eggNOG; COG0134; Bacteria.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_007713_3_1_6; -.
DR   OMA; YDIIGIN; -.
DR   OrthoDB; 1789381at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000000416; 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; -; 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..451
FT                   /note="Tryptophan biosynthesis protein TrpCF"
FT                   /id="PRO_0000154272"
FT   REGION          1..256
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          257..451
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ   SEQUENCE   451 AA;  51594 MW;  88FD5F0E84FA7B71 CRC64;
     MQETILNKII KDKIDWIKYR KKIQPLIKFK NKINKETRNF YNSLKEKRPF FILECKKSSP
     SLGIIRKKFN LIEIANIYKN YASAISVLTD EKYFHGNIEY INVVRRCVSQ PILCKDFFID
     SYQVYLARYY SADAILLMLS VLNDSQYLEL SRIAKELNMG VLTEINNIKE LKRAIKLNAS
     VIGINNRNLH DLSIDLNRTR TLSPLIKNKI IVSESGIKKN HQIKELSNIV HGFLIGSSLM
     YRTNLETNIK SLIIGDNKVC GLTRIIDAKI VESCGAVYGG LIFADNSLRK TNEKIAEKMI
     FENNLRFIGV FQNQDIEKIV NIAQRLSLYA VQLHGSENQK YINILRKKLC KKIKIWKAFS
     IQSTLPLLNW DHIDKYIFDS GSGGTNKTFN WSILKGSILE NVILAGGINT DNVLIASQLN
     CSGLDFNSGV EKSPGIKDHK KISLIFKKLT F