A0A1Y0N1Z5 · A0A1Y0N1Z5_9FLAO

  • Protein
    2-amino-3-ketobutyrate coenzyme A ligase
  • Gene
    kbl
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.

Caution

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

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Note: Binds 1 pyridoxal phosphate per subunit.

Pathway

Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 2/2.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site136substrate
Binding site185pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site241-244pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site274-275pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site368substrate

GO annotations

AspectTerm
Molecular Functionglycine C-acetyltransferase activity
Molecular Functionpyridoxal phosphate binding
Biological Processbiosynthetic process
Biological ProcessL-threonine catabolic process to glycine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    2-amino-3-ketobutyrate coenzyme A ligase
  • EC number
  • Short names
    AKB ligase
  • Alternative names
    • Glycine acetyltransferase

Gene names

    • Name
      kbl
    • ORF names
      BTO07_13700

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SA4-12
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae

Accessions

  • Primary accession
    A0A1Y0N1Z5

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue244N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain43-386Aminotransferase class I/classII large

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    397
  • Mass (Da)
    43,975
  • Last updated
    2017-08-30 v1
  • Checksum
    B67BEC9D6438B44F
MYGKIKDTLKKEIQEIKDAGLYKSERIITSSQDAVIKISTGEEVINFCANNYLGLSNHPEVIQAAKDTMDTHGFGMSSVRFICGTQDIHKQLEKTIANFYTTEDTILYAAAFDANGGVFEPLLTKEDAIISDSLNHASIIDGVRLCKAARYRYNNNDMTSLEEQLIEANKQNHRFKIIVTDGVFSMDGIVAKLDEICDLADKYDALVMVDECHATGFIGKTGRGTVELKNVMDRVDIVTGTLGKALGGAMGGYTTGKKEIIEILRQRSRPYLFSNSLAPGIVGATLKVFDLISDDTSLRDKLEWNTNYFRTEMEKAGFDLVGADAAIVPVMLYDAKLSQVMANKLLEKGIYVIGFFFPVVPKEKARIRVQLSAAHTKDHLNKAITAFIEVGRELKII

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP019334
EMBL· GenBank· DDBJ
ARV16131.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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