A0A0H2YX35 · A0A0H2YX35_ECOK1

  • Protein
    Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
  • Gene
    bioA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.

Catalytic activity

Cofactor

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

Pathway

Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.

Features

Showing features for site, binding site.

Type
IDPosition(s)Description
Site17Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM
Binding site52substrate
Binding site112-113pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site144substrate
Binding site245pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site274substrate
Binding site307substrate
Binding site308-309pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site391substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
Molecular Functionpyridoxal phosphate binding
Biological Processbiotin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
  • EC number
  • Alternative names
    • 7,8-diamino-pelargonic acid aminotransferase
      (DAPA AT
      ; DAPA aminotransferase
      )
    • 7,8-diaminononanoate synthase
      (DANS
      )
    • Diaminopelargonic acid synthase

Gene names

    • Name
      bioA
    • ORF names
      APECO1_1315

Organism names

  • Taxonomic identifier
  • Strain
    • APEC O1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A0H2YX35

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue274N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    429
  • Mass (Da)
    47,229
  • Last updated
    2015-09-16 v1
  • Checksum
    0E6C7784C13AC22E
MTTDDLAFDQRHIWHPYTSMTSPLPVYPVASAEGCELILSDGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAMKMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNSMHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAAHRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKMCDREGILLIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAANASLAILESGDWQHQVAAIEAQLREQLAPACDAEMVADVRVLGAIGVVETTRPVNMAALQKFFVEQGVWIRPFGKLIYLMPPYIILPQQLQRLTAAVNRAVQDETFFCQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000468
EMBL· GenBank· DDBJ
ABJ00156.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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