A0A078RYC7 · A0A078RYC7_BACUN

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.

Type
IDPosition(s)Description
Binding site62[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site66[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site69[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site106[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site138[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site198[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site268[2Fe-2S] cluster (UniProtKB | ChEBI)
Site333Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM
Binding site368substrate
Binding site428-429pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site461substrate
Binding site562pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site591substrate
Binding site624substrate
Binding site625-626pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site710substrate

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

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
    Biotin synthase
  • EC number

Gene names

    • Name
      bioB
    • Synonyms
      bioA
    • ORF names
      M094_1144

Organism names

Accessions

  • Primary accession
    A0A078RYC7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue591N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain44-273Radical 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
    744
  • Mass (Da)
    83,231
  • Last updated
    2014-10-29 v1
  • Checksum
    9419DEBE59A293D2
MTLQKLKEQVLRGSHISKEEAEWLAVQPDKEALYEAAHEITRGLASEEFDMCSIINAKSGRCPENCKWCAQSSHYKTQADVYDLVDKEECLRHARHNEAQGVARFSLVTSGRKPSSRNMEKLCEAARHMRRHSSIQLCASLGLLNEDEMRALHDAGITRYHCNLETAPSYFPQLCSTHTQEEKLRTLQAARNVGMDICSGGIIGMGESMEQRIEFAFTLRELEVQSIPINLLSPIPGTPLERQAPLSEEEILTTIALFRFINPTAFLRFAGGRSQLSKEAVKQALHIGINSAIVGDLLTTLGSKVSEDKVLIENAGYRFCGSQFDREHLWHPYTSTTNPLPVYKVKHAEGATITLESGETLVEGMSSWWCAVHGYNHPTLNRAAEEQLGKMSHVMFGGLTHDPAIELGQLLLPLVPPSMQKIFYADSGSVAVEVALKMAVQYWYGKGKAKKNNFVTIRSGYHGDTWNAMSVCDPVTGMHSLFGASLPVRYFVPQPRSRFHGEWDERDTVELRKLVEEHHEELAALILEPVVQGAGGMWFYHPQYLREAAQICKEHGLLLIFDEIATGFGRTGKLFAWEHAGVEPDIMCIGKAITGGYMTLSAVLTTNEVADTISNHTPEVFMHGPTFMGNPLACAVACASVKLLTSPEYDWQGKVTRISRQLQEELEPARRLPQVTDVRVLGAIGVIETKKPVDMAWMQKRFVEEGIWVRPFGRLVYLMPPFIIEPEQLRKLTGGLMKIIQEMN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JNHN01000174
EMBL· GenBank· DDBJ
KDS50219.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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