A0A5M5M544 · A0A5M5M544_BACOV

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

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 site125[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site129[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site132[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site169[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site201[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site261[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site331[2Fe-2S] cluster (UniProtKB | ChEBI)
Site396Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM
Binding site431substrate
Binding site491-492pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site524substrate
Binding site625pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site654substrate
Binding site687substrate
Binding site688-689pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site771substrate

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
      bioA
    • Synonyms
      bioB
    • ORF names
      F3B85_14895

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BIOML-A41
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides

Accessions

  • Primary accession
    A0A5M5M544

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue654N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain107-336Radical 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
    804
  • Mass (Da)
    90,081
  • Last updated
    2020-06-17 v1
  • Checksum
    1550EF5D88CFC8EC
MKQQRHIQTTRTLLSRFRYWGRKNYAAFASMGREFQIGHLHTNVVDVALRKQNAAQTIPYHTFMTLQEIKDQVLAGIDISPDQAAWLANMADSEALYAAAHEITVARASHEFDMCSIINAKSGRCPENCKWCAQSSHYQTKAEIYDLLPAEECLRQAQYNEAQDVNRFSLVTSGRKPSPKQITQLCDTVRYMRRHSSIQLCASLGLLNEEELRSLHEAGITRYHCNLETAPSYFSKLCSTHTQEQKLATLDAARRVGMDICCGGIIGMGETMEQRIEFAFTLAELNVQSIPINLLSPIPGTPLENEQPLSEEEILKTIALFRFINPTAFLRFAGGRSQLSSEAMHKALYIGINSAIVGDLLTTLGSKVSEDKKMIQEEGYHFADSQFDREHIWHPYTSTTDPLPVYKVKRADGATITLEDGRTLIDGMSSWWCAVHGYNHPVLNQAAKEQLDKISHVMFGGLTHDPAIELGKLLLPLVPSSMQKIFYADSGSVAVEVALKMAVQYWYAAGKPEKNNFVTIRSGYHGDTWNAMSVCDPVTGMHSLFGSALPVRYFVPSPTSRFDGEWNPKDILPLQEMIEKHSKELAALILEPVVQGAGGMWFYHPQYLREAEKLCRKHDILLIFDEIATGFGRTGKLFAWEHAGVEPDIMCIGKALTGGYMTLSAVLTSNRIADTISNHAPGAFMHGPTFMGNPLACAVACASVRLLLESGWQKNVKRIETQLKEELAPAREFPEVADVRILGAIGVIEMKRPVNMAYMQRRFVEERIWVRPFGKLVYLMPPFIITSEQLSKLTSGLLKVIQKR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VWGP01000010
EMBL· GenBank· DDBJ
KAA4535150.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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