B8CX89 · DAPAT_HALOH

Function

function

Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site13substrate
Binding site38substrate
Binding site67pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site101-102pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site102substrate
Binding site126pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site126substrate
Binding site176pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site176substrate
Binding site207pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site235-237pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site246pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site364substrate

GO annotations

AspectTerm
Molecular FunctionL,L-diaminopimelate aminotransferase activity
Molecular Functionpyridoxal phosphate binding
Biological Processlysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    LL-diaminopimelate aminotransferase
  • EC number
  • Short names
    DAP-AT
    ; DAP-aminotransferase
    ; LL-DAP-aminotransferase

Gene names

    • Name
      dapL
    • Ordered locus names
      Hore_11560

Organism names

Accessions

  • Primary accession
    B8CX89

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_10001868701-389LL-diaminopimelate aminotransferase
Modified residue238N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    389
  • Mass (Da)
    43,768
  • Last updated
    2009-03-03 v1
  • Checksum
    C89C8D523F281C4E
MENADRIKNLPPYLFAEIDKMIARAKKEGVDVISFGIGDPDQPTPDNIINKMIEAVKDPSTHSYPSYEGMYEYRKTVADWYKNNYGRELDPDKEVVSLIGSKEGIAHLPFCYINPGDIALVPDPGYPVYKTSVLLAGGKPVQVPLVEENNFLPDLKAIDEDIARKAKLFFINYPNNPTGAIAPEEFYEELIDFADKYDIIIAHDAAYSEIGLDGYNPPSFMQFEGAKKVGIEFNSLSKPFNMTGWRVGWAVGRSDVIESLGRIKTNIDSGIFEAIQYAGIEALTGPEDNIEKMTELYSKRRDLLVEGLRELGWEVPVNKATFYIWAKVPEGYNSTEFSTHVFEKTGIFFTPGNGYGEFGEGYVRIALTVTEERIKEALERLKNSDIKFK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001098
EMBL· GenBank· DDBJ
ACL69908.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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