A0A955S3P8 · A0A955S3P8_UNCOM

Function

function

Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
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

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.
Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site11-16ATP (UniProtKB | ChEBI)
Binding site15Mg2+ (UniProtKB | ChEBI)
Active site36
Binding site44ATP (UniProtKB | ChEBI)
Binding site44Mg2+ (UniProtKB | ChEBI)
Binding site105Mg2+ (UniProtKB | ChEBI)
Binding site105-108ATP (UniProtKB | ChEBI)
Binding site165-166ATP (UniProtKB | ChEBI)
Site243Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM
Binding site340-341pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site373substrate
Binding site472pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site501substrate
Binding site536substrate
Binding site537-538pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site631substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
Molecular FunctionATP binding
Molecular Functiondethiobiotin synthase activity
Molecular Functionmagnesium ion binding
Molecular Functionpyridoxal phosphate binding
Biological Processbiotin biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
  • EC number
  • Alternative names
    • 7,8-diamino-pelargonic acid aminotransferase
    • 7,8-diaminononanoate synthase
    • Diaminopelargonic acid synthase
      (DANS
      ; DAPA AT
      ; DAPA aminotransferase
      )
  • Recommended name
    ATP-dependent dethiobiotin synthetase BioD
  • EC number
  • Alternative names
    • DTB synthetase
    • Dethiobiotin synthase
      (DTBS
      )

Gene names

    • Name
      bioA
    • Synonyms
      bioD
    • ORF names
      KC684_00365

Organism names

Accessions

  • Primary accession
    A0A955S3P8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue501N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the dethiobiotin synthetase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    667
  • Mass (Da)
    74,919
  • Last updated
    2023-02-22 v1
  • Checksum
    F27856AA2D6103A8
MNYFITGTDTDVGKTIVTYVLGLLLQEQGHNVGVMKPVQCAGEDAEFLVNALNIKDAFHNVNPFYTEEPLSPHLAFHRAKKTINISQILKSYQILSECHDLMLVEGAGGLMVPLKKNYLVADLIRDLDLDVIVVSRLGLGAINHALLTIRQAQDYGLNVKGVVFSEANNCKKGLAESNNPEAIEEYGGVPVLGKVPFMKNLSRTQVIQKCKDKINVRALLKKPSQQKTKQLVKDDQQYVWHPFTQMKDWMNDEPLIIEKGQGSYLIDTEGRRYLDGVSSLWVNVHGHHHRDIDHAVKSQVNHLAHSTLLGLSNPPAIELAKELVKITPKGLDKVFYSDSGSTAVEIALKLAYQYWQNIGQPKKINIVHLANSYHGDTLGSVSVGGIDLFHKVYRHLRFQTIKLDFPDCYRNQDVDQALDNLEQLFQQRHTEIAAFVVEPIVQGAAGMIMWPKGVLKRMADVCRKYDVLFITDEVATGFGRTGSMFACEHEDVQPDFLCLAKGITGGYLPLAATLTTKRVFDGFLFNYKDLKTFFHGHTYTGNPLACAAALANLKIFKKERTLTKLAPKIKYLDKSLKMFYNLPHVGDVRQRGFMVGIELVQNKSSKTPYPYEWQMGAKVCQKVRERGVILRPLGNVIVLMPPLSISKEELKELLDVTYWALELITGE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAGQKQ010000003
EMBL· GenBank· DDBJ
MCA9404966.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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