A0A4Q7E1M1 · A0A4Q7E1M1_9CYAN

  • Protein
    (S)-8-amino-7-oxononanoate synthase BioU
  • Gene
    bioU
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site18-22NAD+ (UniProtKB | ChEBI)
Binding site63NAD+ (UniProtKB | ChEBI)
Active site129Nucleophile
Binding site195-196NAD+ (UniProtKB | ChEBI)
Active site199Proton acceptor
Active site203Proton 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
      DYY88_19545

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Lakshadweep
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Leptolyngbyales > Leptolyngbyaceae > Leptolyngbya group > Leptolyngbya > Leptolyngbya iicbica

Accessions

  • Primary accession
    A0A4Q7E1M1

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue129Allysine

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain14-74Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase C-terminal

Sequence similarities

Belongs to the BioU family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    336
  • Mass (Da)
    35,979
  • Last updated
    2019-07-31 v1
  • Checksum
    4E986C76B31D1543
MNSQTIASQSPIAVGVLGFGGLGQAATRVLMPKTEMQLVAAADKQGYVYDARGLEPQTCIEAYRDRGSVGYVESGGVLSQQSIADLIQAAPNVQGYFLALPNLPNTFMASVVQQFIASGWRGVLVDALKRTSAMEQIYALRDELQAAGITYMTGCGATPGLLTAAATVAAQSYTEIHSVKITFGVGIANWEAYRATIREDIAHMPEYDVDSARAMSDEEVAALLDRTDGILQLENMEHADDLMLELAGICDRDQVTVGGIVDTRNSKKPLSTNVQVTGRTFEGKISTHTFTLGDETSMAANVCGPAFGYLKAGITLHQRGQHGLYTAAEVMPQFVR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QVFV01000006
EMBL· GenBank· DDBJ
RZM76085.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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