A5ZUL4 · A5ZUL4_9FIRM

Function

function

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.

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.
[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.

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site62[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site62[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site66[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site66[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site68S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site69[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site69[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site74Fe3+ (UniProtKB | ChEBI)
Binding site106[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site138[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site163S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site165S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site198[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site233S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site268[2Fe-2S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionbiotin synthase activity
Molecular Functioniron ion binding
Biological Processbiotin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Biotin synthase
  • EC number

Gene names

    • Name
      bioB
    • ORF names
      RUMOBE_02699

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ATCC 29174
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Blautia

Accessions

  • Primary accession
    A5ZUL4

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain44-270Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. Biotin synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    327
  • Mass (Da)
    36,286
  • Last updated
    2007-07-24 v1
  • Checksum
    96AB0337ACCCD345
MNPLTLAQEIIDGRRITREDDLSFFLTCDLDELCEGADRIREACIGDKVDLCSIINGRSGRCPEDCKYCAQSAHHHTSCEVYNFLPEEKILEACKMNESEGVDRFSIVTAGKALTGKEFDQAIHAYETMHRECKIDLCASMGFISAEQLHRLHEAGVTSYHHNIETSRRNFPNICTTHTYDMKIETLKKVKAEGMCACSGGIIGMGETWEDRLDMAISLAELGIDSIPINALMPIPGTPLEHLPELSEPDILRTIAFFRYINPEANIRLAAGRALLTNDGETAFKAGASASITGNMLTTVACATIRSDRKMLADMGRDVTPEYWKEV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAVO02000012
EMBL· GenBank· DDBJ
EDM86794.1
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.
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