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A0A2R6HWQ7 · A0A2R6HWQ7_9EURY

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

Lacks conserved residue(s) required for the propagation of feature annotation.
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.

Type
IDPosition(s)Description
Binding site10-14NAD+ (UniProtKB | ChEBI)
Active site136Nucleophile
Binding site203-204NAD+ (UniProtKB | ChEBI)
Active site207Proton acceptor
Active site211Proton donor and proton acceptor

GO annotations

AspectTerm
Molecular FunctionNAD binding
Molecular FunctionNADP binding
Molecular Functiontransaminase activity
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
      BRC94_13005

Organism names

Accessions

  • Primary accession
    A0A2R6HWQ7

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue136Allysine

Interaction

Subunit

Monomer.

Family & Domains

Sequence similarities

Belongs to the BioU family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    342
  • Mass (Da)
    36,316
  • Last updated
    2018-06-20 v1
  • MD5 Checksum
    2A484BAF577F60B743D060CF6C6131F2
MDDVRFAVLGTGGIGRRTLEVSTEKAGVTPVAACDRHGIAVDRDGLDIEELLAATEGNVASDGGAGAVKQHGELSGVAASAQARPTETPIDDVIAESDDLDAVLIALPNLEHDFIPRVAERFADAGYEGVLVDVLKRSRVIGMLDDREATLREAGITFVCGAGATPGFLTGAAALAAQSFVEVEAVEIWWGVGLKSGYRDNRGTVREDIAHLDGYDIETARELTDEEIEEIVDAHDGVLEFHDMEHADDVLLERAGICDAEDVTVGGVLDVRSDEKPTTTTVRVTGRTFDGERGTNTFELDDDTSMAANVNGPALGYLKAAVRRNRTGDYGVYGPAELMPGF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PXRR01000073
EMBL· GenBank· DDBJ
PSP96358.1
EMBL· GenBank· DDBJ
Genomic DNA

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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