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trpC fused indole-3-glycerol phosphate synthase/phosphoribosylanthranilate isomerase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945519, updated on 14-Nov-2024

Summary

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Official Symbol
trpC
Official Full Name
fused indole-3-glycerol phosphate synthase/phosphoribosylanthranilate isomerase
Primary source
ECOCYC:EG11026
Locus tag
b1262
See related
ASAP:ABE-0004238
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1256; trpCF; trpF
Summary
The N-terminal synthase is the TrpC domain and the C-terminal isomerase domain is the TrpF domain. [More information is available at EcoGene: EG11026]. Bifunctional phosphoribosylanthranilate isomerase / indole-3-glycerol phosphate synthase (TrpC) carries out the third and fourth steps in the tryptophan biosynthesis pathway. [More information is available at EcoCyc: EG11026].
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Genomic context

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Sequence:
NC_000913.3 (1318427..1319788, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene stress-induced bacterial acidophilic repeat motifs-containing protein YciG Neighboring gene tryptophan synthase subunit alpha Neighboring gene tryptophan synthase subunit beta Neighboring gene anthranilate synthase subunit TrpD Neighboring gene anthranilate synthase subunit TrpE

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Indoleglycerol phosphate synthase-phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains. Eberhard M, et al. Biochemistry, 1995 Apr 25. PMID 7727400
  2. Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution. Wilmanns M, et al. J Mol Biol, 1992 Jan 20. PMID 1738159
  3. Crystallization and structure solution at 4 A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue. Wilmanns M, et al. Protein Eng, 1990 Jan. PMID 2184433
  4. Structure of the trpC cistron specifying indoleglycerol phosphate synthetase, and its localization in the tryptophan operon of Escherichia coli. Smith OH. Genetics, 1967 Sep. PMID 4865047, Free PMC Article
  5. N-(5'-phosphoribosyl)anthranilate isomerase-indol-3-ylglycerol phosphate synthetase of tryptophan biosynthesis. Relationship between the two activities of the enzyme from Escherichia coli. Creighton TE. Biochem J, 1970 Dec. PMID 4924490, Free PMC Article

See all (40) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. analysis of the unfolding pathway of ePRAI, a (beta/alpha)8-barrel protein, by molecular dynamics simulations
    Title: A detailed unfolding pathway of a (beta/alpha)8-barrel protein as studied by molecular dynamics simulations.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables carbon-carbon lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables carboxy-lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables indole-3-glycerol-phosphate synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables indole-3-glycerol-phosphate synthase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables indole-3-glycerol-phosphate synthase activity IEA
Inferred from Electronic Annotation
more info
  
enables isomerase activity IEA
Inferred from Electronic Annotation
more info
  
enables phosphoribosylanthranilate isomerase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables phosphoribosylanthranilate isomerase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphoribosylanthranilate isomerase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in alpha-amino acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in aromatic amino acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in indolalkylamine metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in tryptophan biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in tryptophan biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within tryptophan biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in tryptophan metabolic process IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
fused indole-3-glycerol phosphate synthase/phosphoribosylanthranilate isomerase
NP_415778.3

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1318427..1319788 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415778.3 fused indole-3-glycerol phosphate synthase/phosphoribosylanthranilate isomerase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415778.3

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A2X5H0P3, A0AAE9TQE7, Q2XN48
    Conserved Domains (1) summary
    PRK09427
    Location:1 → 453
    PRK09427; bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF
Nucleotide Protein
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Gene LinkOut

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