ID TRPC_ECOLI Reviewed; 453 AA. AC P00909; P78059; P78234; P94704; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 19-MAR-2014, sequence version 4. DT 24-JAN-2024, entry version 188. 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=trpF; OrderedLocusNames=b1262, JW1254; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7007653; DOI=10.1016/0022-2836(80)90261-2; RA Christie G.E., Platt T.; RT "Gene structure in the tryptophan operon of Escherichia coli. Nucleotide RT sequence of trpC and the flanking intercistronic regions."; RL J. Mol. Biol. 142:519-530(1980). RN [2] RP SEQUENCE REVISION TO 95 AND 399. RX PubMed=6355484; DOI=10.1016/s0022-2836(83)80136-3; RA Horowitz H., van Arsdell J., Platt T.; RT "Nucleotide sequence of the trpD and trpC genes of Salmonella RT typhimurium."; RL J. Mol. Biol. 169:775-797(1983). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7038627; DOI=10.1093/nar/9.24.6647; RA Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., RA Horowitz H., van Cleemput M., Wu A.M.; RT "The complete nucleotide sequence of the tryptophan operon of Escherichia RT coli."; RL Nucleic Acids Res. 9:6647-6668(1981). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8095913; DOI=10.1093/genetics/133.3.455; RA Milkman R., Bridges M.M.; RT "Molecular evolution of the Escherichia coli chromosome. IV. Sequence RT comparisons."; RL Genetics 133:455-468(1993). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [8] RP PROTEIN SEQUENCE OF 1-8. RC STRAIN=K12 / BW25113; RX PubMed=23908556; DOI=10.1074/mcp.m113.029165; RA Krug K., Carpy A., Behrends G., Matic K., Soares N.C., Macek B.; RT "Deep coverage of the Escherichia coli proteome enables the assessment of RT false discovery rates in simple proteogenomic experiments."; RL Mol. Cell. Proteomics 12:3420-3430(2013). RN [9] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SEQUENCE REVISION TO 320. RX PubMed=1738159; DOI=10.1016/0022-2836(92)90665-7; RA Wilmanns M., Priestle J.P., Niermann T., Jansonius J.N.; RT "Three-dimensional structure of the bifunctional enzyme RT phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from RT Escherichia coli refined at 2.0-A resolution."; RL J. Mol. Biol. 223:477-507(1992). RN [11] RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 258-453. RX PubMed=2184433; DOI=10.1093/protein/3.3.173; RA Wilmanns M., Schlagenhauf E., Fol B., Jansonius J.N.; RT "Crystallization and structure solution at 4-A resolution of the RT recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate RT isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli RT complexed to a substrate analogue."; RL Protein Eng. 3:173-180(1990). 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. 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. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V00366; CAA23664.1; -; Genomic_DNA. DR EMBL; V00372; CAA23673.1; -; Genomic_DNA. DR EMBL; J01714; AAA57299.1; -; Genomic_DNA. DR EMBL; U23489; AAB60033.1; -; Genomic_DNA. DR EMBL; U00096; AAC74344.3; -; Genomic_DNA. DR EMBL; AP009048; BAA14794.1; -; Genomic_DNA. DR PIR; A64874; GWEC. DR RefSeq; NP_415778.3; NC_000913.3. DR RefSeq; WP_000983871.1; NZ_SSZK01000031.1. DR PDB; 1JCM; X-ray; 2.10 A; P=2-260. DR PDB; 1PII; X-ray; 2.00 A; A=2-453. DR PDB; 2KZH; NMR; -; A=256-385. DR PDBsum; 1JCM; -. DR PDBsum; 1PII; -. DR PDBsum; 2KZH; -. DR AlphaFoldDB; P00909; -. DR BMRB; P00909; -. DR SMR; P00909; -. DR BioGRID; 4260122; 4. DR BioGRID; 849893; 4. DR IntAct; P00909; 7. DR STRING; 511145.b1262; -. DR DrugBank; DB03543; 1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate. DR jPOST; P00909; -. DR PaxDb; 511145-b1262; -. DR EnsemblBacteria; AAC74344; AAC74344; b1262. DR GeneID; 945519; -. DR KEGG; ecj:JW1254; -. DR KEGG; eco:b1262; -. DR PATRIC; fig|511145.12.peg.1312; -. DR EchoBASE; EB1019; -. DR eggNOG; COG0134; Bacteria. DR eggNOG; COG0135; Bacteria. DR HOGENOM; CLU_007713_1_2_6; -. DR InParanoid; P00909; -. DR BioCyc; EcoCyc:PRAI-IGPS; -. DR BioCyc; MetaCyc:PRAI-IGPS; -. DR BRENDA; 5.3.1.24; 2026. DR SABIO-RK; P00909; -. DR UniPathway; UPA00035; UER00042. DR UniPathway; UPA00035; UER00043. DR EvolutionaryTrace; P00909; -. DR PRO; PR:P00909; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IDA:EcoCyc. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IDA:EcoCyc. DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:EcoCyc. 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 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Decarboxylase; Direct protein sequencing; Isomerase; Lyase; KW Multifunctional enzyme; Reference proteome; Tryptophan biosynthesis. FT CHAIN 1..453 FT /note="Tryptophan biosynthesis protein TrpCF" FT /id="PRO_0000154277" FT REGION 1..257 FT /note="Indole-3-glycerol phosphate synthase" FT REGION 258..453 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT CONFLICT 31 FT /note="Missing (in Ref. 3; CAA23673)" FT /evidence="ECO:0000305" FT CONFLICT 95 FT /note="Q -> R (in Ref. 1; CAA23664/AAA57299 and 3; FT CAA23673)" FT /evidence="ECO:0000305" FT CONFLICT 285 FT /note="Missing (in Ref. 3; CAA23673)" FT /evidence="ECO:0000305" FT CONFLICT 294 FT /note="V -> D (in Ref. 3; CAA23673)" FT /evidence="ECO:0000305" FT CONFLICT 330 FT /note="A -> V (in Ref. 1; CAA23664/AAA57299 and 3; FT CAA23673)" FT /evidence="ECO:0000305" FT CONFLICT 399 FT /note="S -> T (in Ref. 1; CAA23664/AAA57299, 3; CAA23673 FT and 4; AAB60033)" FT /evidence="ECO:0000305" FT HELIX 5..23 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 40..44 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:1PII" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 71..78 FT /evidence="ECO:0007829|PDB:1PII" FT TURN 79..81 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 83..88 FT /evidence="ECO:0007829|PDB:1PII" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 100..107 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 112..116 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 121..129 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 133..138 FT /evidence="ECO:0007829|PDB:1PII" FT TURN 139..141 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 144..156 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 168..176 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 180..187 FT /evidence="ECO:0007829|PDB:1PII" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 197..206 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 210..216 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 221..227 FT /evidence="ECO:0007829|PDB:1PII" FT TURN 228..230 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 238..241 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 246..255 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 266..275 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 278..283 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 307..314 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 330..334 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:2KZH" FT HELIX 340..349 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 354..361 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 376..381 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 392..395 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 403..408 FT /evidence="ECO:0007829|PDB:1PII" FT TURN 411..413 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 414..418 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 423..427 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:1PII" FT STRAND 432..434 FT /evidence="ECO:0007829|PDB:1PII" FT HELIX 440..451 FT /evidence="ECO:0007829|PDB:1PII" SQ SEQUENCE 453 AA; 49492 MW; 09D5DA2353291F33 CRC64; MMQTVLAKIV ADKAIWVEAR KQQQPLASFQ NEVQPSTRHF YDALQGARTA FILECKKASP SKGVIRDDFD PARIAAIYKH YASAISVLTD EKYFQGSFNF LPIVSQIAPQ PILCKDFIID PYQIYLARYY QADACLLMLS VLDDDQYRQL AAVAHSLEMG VLTEVSNEEE QERAIALGAK VVGINNRDLR DLSIDLNRTR ELAPKLGHNV TVISESGINT YAQVRELSHF ANGFLIGSAL MAHDDLHAAV RRVLLGENKV CGLTRGQDAK AAYDAGAIYG GLIFVATSPR CVNVEQAQEV MAAAPLQYVG VFRNHDIADV VDKAKVLSLA AVQLHGNEEQ LYIDTLREAL PAHVAIWKAL SVGETLPARE FQHVDKYVLD NGQGGSGQRF DWSLLNGQSL GNVLLAGGLG ADNCVEAAQT GCAGLDFNSA VESQPGIKDA RLLASVFQTL RAY //