A0A517XUC4 · A0A517XUC4_9BACT

  • Protein
    Multifunctional fusion protein
  • Gene
    bioA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

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.

Type
IDPosition(s)Description
Binding site16Mg2+ (UniProtKB | ChEBI)
Active site34
Binding site38substrate
Binding site42ATP (UniProtKB | ChEBI)
Binding site42Mg2+ (UniProtKB | ChEBI)
Binding site99Mg2+ (UniProtKB | ChEBI)
Binding site99-102ATP (UniProtKB | ChEBI)
Site237Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM
Binding site272substrate
Binding site333-334pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site366substrate
Binding site454pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site483substrate
Binding site517substrate
Binding site518-519pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site606substrate

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

Enzyme and pathway databases

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
      ETAA1_30650

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ETA_A1
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Gemmatales > Gemmataceae > Urbifossiella

Accessions

  • Primary accession
    A0A517XUC4

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue483N6-(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
    641
  • Mass (Da)
    68,127
  • Last updated
    2019-10-16 v1
  • Checksum
    AACDB330964E960D
MTGFVVVGTDTDAGKTAFSLMFLAAFPDTFAYWKPVETGDSDAEKVRRLVPRAVVLPPLARFSEPVAPVLAARREGRAMPGVADILAARPSADRPLLIETFGGPMSPLTDDVLQLDLIRAFALPVVLVSSAAVGAVARTLQAAAALEHAGLRPVAVALTGADDAFACDQITRRLGGIPVACHEFPAGEWTRDSLAAAAERSRWALQRVEPIVRAGPTFGGRPTDIAAADARAVWHPYTPLQSPDAPLAVAAADDEFLTLDDGRRLIDGISSWWTILHGHRPPAIMQAVRDATHQLDHVLFAGATHPAAVELATSLLGSMPWGPGGRVFYSDNGSTAVEVALKMAYQAWCHRGEAGRTLFVGFEHGYHGDTFGAMSLSRDPVFFGRFEPLLFRALQVPLSADALDAALTHHAGEVAGVLVEPLVQGAGGMRLHTPEELRALFEVTRRHGVPFIADEVMTGFGRTGSLWAFEQAGIAPDLVCAAKGITGGVLPLAATLASPEVVAAFDTADRTRTFFHGHSFTANPIACAAAVASWRLLQTGRWRTDVRRIEAHWLAAAAGLRKLHGVKDARVRGLILAAELDVPGGYLADVGRAMRLAALERGVLLRPLGNVLYALPPLCTSDDSLARIADAMVHAVRSCGL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036273
EMBL· GenBank· DDBJ
QDU21100.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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