A0A1B7W0L3 · A0A1B7W0L3_APHFL

Function

function

A 'suicide' enzyme that participates in biotin synthesis. Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function equivalent to the cannonical BioA reaction and the first half-reaction of BioD. The cellular requirement for biotin is thought be low enough that this single turnover enzyme supplies a sufficient amount of the cofactor. Overall it catalyzes three reactions: formation of a covalent linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)+.

Miscellaneous

In cannonical biotin synthesis a pimeloyl-conjugate is transformed into biotin by the subsequent action of BioF, BioA, BioD and BioB. This enzyme replaces BioA and performs the first half-reaction of BioD.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Cofactor biosynthesis; biotin biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site12-16NAD+ (UniProtKB | ChEBI)
Binding site57NAD+ (UniProtKB | ChEBI)
Active site124Nucleophile
Binding site190-191NAD+ (UniProtKB | ChEBI)
Active site194Proton acceptor
Active site198Proton donor and proton acceptor

GO annotations

AspectTerm
Molecular FunctionNAD binding
Molecular FunctionNADP binding
Molecular Functionoxidoreductase activity
Molecular Functiontransaminase activity
Biological Processamino acid metabolic process
Biological Processbiotin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    (S)-8-amino-7-oxononanoate synthase BioU
  • EC number
  • Alternative names
    • 8-amino-7-oxononanoate carboxylating dehydrogenase

Gene names

    • Name
      bioU
    • ORF names
      AN481_03375

Organism names

Accessions

  • Primary accession
    A0A1B7W0L3

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue124Allysine

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-67Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase C-terminal

Sequence similarities

Belongs to the BioU family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    331
  • Mass (Da)
    35,068
  • Last updated
    2016-11-02 v1
  • Checksum
    B37BF44E37E6BE13
MNTPPLRVGVLGFGGLGQAAAKLLTSKREMILVAVADQKGYAYSTEGLNTQACITTYQTQGTVGYLEPVGTLSNNSIQDLIQATGDTVNGYFLALPNLPNDFIPSVAKEFIKAAWKGVLVDAIKRTSAVEQLLAMKNELQAAGITYMTGCGATPGLLTAAAALAAQSYAEIHNVEITFGVGIANWEAYRATVREDIGHISGYSVEAAKAMTDAEVEALLDQTNGVLTLKNMEHADDIMLEIAGICSRDRVTVGGVVDTRNPKKPLSTNVKVTGRTFEGKISTHTFTLGDETSMAANVCGPAFGYLKAGQELHQRGVSGLFTAAEIMPKFVK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LJOY01000007
EMBL· GenBank· DDBJ
OBQ26755.1
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