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trpB tryptophan synthase subunit beta [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945768, updated on 30-Jul-2025
Official Symbol
trpB
Official Full Name
tryptophan synthase subunit beta
Primary source
ECOCYC:EG11025
Locus tag
b1261
See related
ASAP:ABE-0004234
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1255
Summary
otherPDB (S. typhimurium): [More information is available at EcoGene: EG11025]. The TrpB polypeptide functions as the subunit of the tetrameric (2-2) tryptophan synthase complex. [More information is available at EcoCyc: EG11025].
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Sequence:
NC_000913.3 (1317222..1318415, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF892 domain-containing protein YciF Neighboring gene stress-induced bacterial acidophilic repeat motifs-containing protein YciG Neighboring gene tryptophan synthase subunit alpha Neighboring gene fused indole-3-glycerol phosphate synthase/phosphoribosylanthranilate isomerase Neighboring gene anthranilate synthase subunit TrpD Neighboring gene anthranilate synthase subunit TrpE

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Large conformational changes in the Escherichia coli tryptophan synthase beta(2) subunit upon pyridoxal 5'-phosphate binding. Nishio K, et al. FEBS J, 2010 May. PMID 20370823
  2. Affinity labeling of the pyridoxal phosphate binding site of the beta2 subunit of Escherichia coli tryptophan synthase. Higgins W, et al. J Biol Chem, 1978 Jul 10. PMID 350880
  3. Assignment of the ends of the beta-chain of E. coli tryptophan synthase to the F1 and F2 domains. Crawford IP, et al. Biochem Biophys Res Commun, 1978 Nov 14. PMID 369556
  4. Cooperative and noncooperative binding of pyridoxal 5'-phosphate to tryptophan synthase from Escherichia coli. Bartholmes P, et al. Biochemistry, 1976 Oct 19. PMID 788781
  5. Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility. Zhao GP, et al. J Biol Chem, 1992 Jan 5. PMID 1309752

See all (60) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. determined the crystal structures of apo-tryptophan synthase beta(2) and holo-beta(2) from Escherichia coli at 3.0 and 2.9 A resolutions, respectively.
    Title: Large conformational changes in the Escherichia coli tryptophan synthase beta(2) subunit upon pyridoxal 5'-phosphate binding.
  2. N-terminus verified by Edman degradation on mature peptide
    Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables pyridoxal phosphate binding IDA
Inferred from Direct Assay
more info
 PubMed 
contributes_to tryptophan synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
contributes_to tryptophan synthase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables tryptophan synthase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables tryptophan synthase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in L-tryptophan biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in L-tryptophan biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in L-tryptophan biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within L-tryptophan biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in L-tryptophan metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in amino acid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in aromatic amino acid family biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within aromatic amino acid family biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm NAS
Non-traceable Author Statement
more info
 PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
Preferred Names
tryptophan synthase subunit beta
NP_415777.1

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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
    1317222..1318415 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415777.1 tryptophan synthase subunit beta

    See identical proteins and their annotated locations for NP_415777.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    V9GZL4
    Conserved Domains (1) summary
    PRK04346
    Location:5 → 391
    PRK04346; tryptophan synthase subunit beta; Validated
Nucleotide Protein
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