A0A964IUT7 · A0A964IUT7_9PROT

Function

function

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
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.
Catalyzes two activities which are involved in the biotine biosynthesis: the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism, and 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).

Caution

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:
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
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 2/2.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site80[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site84[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site87[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site124[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site155[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site215[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site287[2Fe-2S] cluster (UniProtKB | ChEBI)
Site381Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM
Binding site416substrate
Binding site476-477pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site509substrate
Binding site603pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site632substrate
Binding site666substrate
Binding site667-668pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site750substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
Molecular Functionbiotin synthase activity
Molecular Functioniron 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
    Biotin synthase
  • EC number

Gene names

    • Name
      bioB
    • Synonyms
      bioA
    • ORF names
      EXQ84_07900

Organism names

  • Taxonomic identifier
  • Strain
    • Baikal-deep-G40
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae

Accessions

  • Primary accession
    A0A964IUT7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue632N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain65-283Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. Biotin synthase family.
In the C-terminal section; belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
In the N-terminal section; belongs to the radical SAM superfamily. Biotin synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    783
  • Mass (Da)
    84,356
  • Last updated
    2023-02-22 v1
  • Checksum
    83B58D1A41BD0669
MKGILNMLPTVEAQTARPQRPNMAHAVGAVRHDWTRGEVRAMFALPFPELMFQAQTVHRMNFDPREVQVSTLLSIKTGGCPEDCGYCPQSARYDTGLTASRLMEVADVLAEAQAAKAAGATRFCMGAAWRSPKDHDVEAVCAMIEGVKALGLESCATLGMLTPQQAIRLKGAGLDYYNHNLDTSAEFYGKIITTRTYADRLDTLANVRDAGINVCCGGIIGMGEGLEDRAGMITTLATLPAHPESVPINLLVQVKGTPLNGTLRLDPLDFVRTIAVARITMPRSMVRLSAGREDMSDEVQALCFLAGANSIFYGDRLLTTPNPGEDHDRALFDRLGLVTMPPREGADWQAAGVSGKRASVTPASNEPDWYESGSPHIWLPYTQMKTAPPPLAVARTHGSRIVLADGRELVDGIASWWTACHGYNHPHIRAAVARQLEIMPHVMLGGLAHEAALTLASRLAGLLPGDLSRVFFCDSGSVAVEVALKMATQYWLNQGVRSRSTFVAFKGGYHGDTIAAMAVSDPDESMHALFKGLLPRHHVIDLPQDDASIAAFDQFLAEKADILAGMVVEPLVQGAGGMLFHNAAVLRCLRAAADRYGLVLICDEIFTGFGRTGAMFACEAAGIVPDIMTLSKALTGGTMTLAATVARGKIFDAFWSEDPAHALMHGPTYMANALACAAANASLDLFEREPRLAQIAAISKTLGQDLEVCRGLPGVKDVRVQGAIGVVEMNHIGDLNGLKRRFVDAGVWVRPFNNIIYLTPAFTIDAEDLAKLTRTIFEVLKLS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SHVO01000061
EMBL· GenBank· DDBJ
MSO73504.1
EMBL· GenBank· DDBJ
Genomic DNA

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