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 05-MAY-2009, entry version 51. 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; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=118110; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95261545; PubMed=7742976; RX 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 CC of tryptophan biosynthetic pathway. The first reaction is CC catalyzed by the isomerase, coded by the trpF domain; the second CC reaction is catalyzed by the synthase, coded by the trpC domain. CC -!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1- CC (2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. CC -!- CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5- CC phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. 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 -!- SIMILARITY: In the C-terminal section; belongs to the trpF family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U09185; AAA92795.1; -; Genomic_DNA. DR HSSP; P00909; 1JCM. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:HAMAP. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00134; fused; 1. DR HAMAP; MF_00135; fused; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013798; Indole-3-glycerol_P_synth. DR InterPro; IPR001468; Indole-3-GPS_central. DR InterPro; IPR001240; PRAI. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF00218; IGPS; 1. DR Pfam; PF00697; PRAI; 1. DR ProDom; PD001511; IGPS; 1. DR PROSITE; PS00614; IGPS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Decarboxylase; Isomerase; Lyase; Multifunctional enzyme; KW Tryptophan biosynthesis. FT CHAIN 1 461 Tryptophan biosynthesis protein trpCF. FT /FTId=PRO_0000154275. FT REGION 1 258 Indole-3-glycerol phosphate synthase. FT REGION 259 461 N-(5'-phosphoribosyl)anthranilate FT 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 //