TRPC_ECOLI
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 03-AUG-2022, entry version 182.
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; Proteobacteria; 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}.
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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_LN832404.1.
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; P00909; -.
DR PRIDE; P00909; -.
DR EnsemblBacteria; AAC74344; AAC74344; b1262.
DR EnsemblBacteria; BAA14794; BAA14794; BAA14794.
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; -; 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 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
