A0A4R5L815 · A0A4R5L815_9BURK

  • 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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

TypeIDPosition(s)Description
Site29Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM
Binding site66substrate
Binding site126-127pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site159substrate
Binding site265pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site294substrate
Binding site328substrate
Binding site329-330pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site418substrate

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
      E1N52_26885

Organism names

  • Taxonomic identifier
  • Strain
    • CNPSo 3008
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Paraburkholderia

Accessions

  • Primary accession
    A0A4R5L815

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue294N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    456
  • Mass (Da)
    50,362
  • Last updated
    2019-07-31 v1
  • Checksum
    AA881AF5D1BE09C1
MNSQSHLAREDRAATDWVARSLRAVWHPCTQMKHHERLPLVAVARGEGPWLHDREGRRYLDAISSWWVNLFGHANASINAALKAQLDTLEHVMLAGCTHEPAVELAERLSARTGGVLGHAFFASDGASAVEIALKMSFHSWRNRGESDKREFVCLANSYHGETIGALGVTDVKLFRDAYDPLLHHAHVVASPDARAAQPGETAADVAARALADVERLFIEREGRIAALIVEPLVQCAAGMAMHDPAYLKGLRALCDRHRVHLIADEIAVGCGRTGTFFACEQADIWPDLLTLSKGISGGYLPLSIVLSRDAIYESFYDDDTTRGFLHSHSYTGNPLACRAALATLDLFERDDVLVTNAHKSAQLRELFDPLAAHPLVRNLRQCGTILAFDVALADPQRAATFSRRFFENALQRELLLRPIGTTVYVMPPYILDNEMQAFLAARTRETFDATVAEDL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SMOD01000023
EMBL· GenBank· DDBJ
TDG05064.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp