U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

dapA 4-hydroxy-tetrahydrodipicolinate synthase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946952, updated on 8-Apr-2026
Official Symbol
dapA
Official Full Name
4-hydroxy-tetrahydrodipicolinate synthase
Primary source
ECOCYC:EG10205
Locus tag
b2478
See related
ASAP:ABE-0008163
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
ECK2474
Summary
DapA levels may be influenced by GroES and GroEL. [More information is available at EcoGene: EG10205]. Lys-161 is the active-site lysine residue of DHDPS. [More information is available at EcoCyc: EG10205].
Try the new Gene page
Try the new Transcripts and proteins table
Sequence:
NC_000913.3 (2598882..2599760, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene phosphoribosylaminoimidazole-succinocarboxamide synthase Neighboring gene outer membrane protein assembly factor BamC Neighboring gene transcriptional regulator GcvR Neighboring gene thiol peroxidase Neighboring gene hydrogenase 4 component A Neighboring gene hydrogenase 4 component B

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Escherichia coli dihydrodipicolinate synthase: characterization of the imine intermediate and the product of bromopyruvate treatment by electrospray mass spectrometry. Borthwick EB, et al. Biochem J, 1995 Jan 15. PMID 7832769, Free PMC Article
  2. Dihydrodipicolinate synthase (DHDPS) from Escherichia coli displays partial mixed inhibition with respect to its first substrate, pyruvate. Dobson RC, et al. Biochimie, 2004 Apr-May. PMID 15194235
  3. The crystal structure of three site-directed mutants of Escherichia coli dihydrodipicolinate synthase: further evidence for a catalytic triad. Dobson RC, et al. J Mol Biol, 2004 Apr 23. PMID 15066435
  4. Insight into the self-association of key enzymes from pathogenic species. Perugini MA, et al. Eur Biophys J, 2005 Jul. PMID 15981001
  5. The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance. Dobson RC, et al. Acta Crystallogr D Biol Crystallogr, 2005 Aug. PMID 16041077

See all (38) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. This study investigated the C-terminal domain of E. coli DHDPS by characterising a C-terminal truncated DHDPS (DHDPS-H225*).
    Title: The C-terminal domain of Escherichia coli dihydrodipicolinate synthase (DHDPS) is essential for maintenance of quaternary structure and efficient catalysis.
  2. to probe the mechanism of dihydrodipicolinate synthase (DHDPS), inhibition of DHDPS by the substrate analog, beta-hydroxypyruvate was studied; crystal structure of DHDPS complexed with beta-hydroxypyruvate was solved
    Title: Conserved main-chain peptide distortions: a proposed role for Ile203 in catalysis by dihydrodipicolinate synthase.
  3. Results suggest that the homotetrameric structure of dihydrodipicolinate synthase reduces dynamic fluctuations present in the dimeric forms and increases specificity for the first substrate, pyruvate.
    Title: Evolution of quaternary structure in a homotetrameric enzyme.
  4. N-terminus verified by Edman degradation on complete protein
    Title: '98 Escherichia coli SWISS-2DPAGE database update.
  5. crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from E. coli are presented to 1.9 and 2.0 A, respectively
    Title: The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance.
  6. evidence that Arg138 of dihydrodipicolinate synthase is responsible for binding the carboxyl of (S)-ASA and is not involved in the mechanism of (S)-lysine inhibition
    Title: Role of arginine 138 in the catalysis and regulation of Escherichia coli dihydrodipicolinate synthase.
  7. The dapA promoter is activated by diaminopimelic acid.
    Title: Expression from the Escherichia coli dapA promoter is regulated by intracellular levels of diaminopimelic acid.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables 4-hydroxy-tetrahydrodipicolinate synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 4-hydroxy-tetrahydrodipicolinate synthase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 4-hydroxy-tetrahydrodipicolinate synthase activity IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables lyase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in L-lysine biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in amino acid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in carboxylic acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol HDA PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
Preferred Names
4-hydroxy-tetrahydrodipicolinate synthase
NP_416973.1

NEW Try the new Transcript table

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
    2598882..2599760 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416973.1 4-hydroxy-tetrahydrodipicolinate synthase

    See identical proteins and their annotated locations for NP_416973.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A8S0FP06
    Conserved Domains (1) summary
    PRK03170
    Location:1 → 292
    PRK03170; dihydrodipicolinate synthase; Provisional
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.