Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A202E7M9 · A0A202E7M9_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 site149Nucleophile
Binding site216-217NAD+ (UniProtKB | ChEBI)
Active site220Proton acceptor
Active site224Proton 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
      B2G88_07585

Organism names

  • Taxonomic identifier
  • Strain
    • CGMCC 1.3597
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natronolimnobius

Accessions

  • Primary accession
    A0A202E7M9

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue149Allysine

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region67-86Disordered
Compositional bias72-86Polar residues

Sequence similarities

Belongs to the BioU family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    355
  • Mass (Da)
    37,376
  • Last updated
    2017-09-27 v1
  • MD5 Checksum
    0A4E783C7648C2535A05903CC5EF92AF
MHEITFAVLGTGGIGRRALEVSQHKAALTPVAACDRHGVALDADGLAVEELLAATEGNIDSGLDDVATDGGDTATSGGSGVKQHGTQRGVVASEQAVATDEPIQAIIDAGAEIDAVLLALPNYEHDFIPRTADRFIEAGYSGVLIDVLKRSRVIGMLEDRRDALEDAGITFICGAGATPGFLTGAAALAAHSFVEVESVDIWWGVGLKSGYEDNRGTVREDIAHLPGYDIETARDLADADIEAIIDDHDGVLEFEDMEHADDVLLERAGICDAADVTVGGILDVRSDEKPTTTTVSVTGRTFDGERATNTFELGDETSMEANVNGPALGYLKAGVRRNRNGEYGVFGPAELLPRF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias72-86Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MWPH01000002
EMBL· GenBank· DDBJ
OVE84271.1
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.
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.
Help