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A0A4R5MHP1 · A0A4R5MHP1_9SPHI

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

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 site183pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site208-211pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site239-242pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site272-273pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site366substrate

GO annotations

AspectTerm
Cellular Componentcytosol
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
      EZJ43_15230

Organism names

  • Taxonomic identifier
  • Strain
    • E01020
  • Taxonomic lineage
    Bacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Pedobacter

Accessions

  • Primary accession
    A0A4R5MHP1

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue242N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain43-384Aminotransferase class I/classII large

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    395
  • Mass (Da)
    43,325
  • Last updated
    2019-07-31 v1
  • MD5 Checksum
    25965375C4639DA7170F7EE67A8B4A8C
MYKTLQPVLQKELEEIENAGLYKKERIIVTPQGADIKVEGGAEVVNFCANNYLGLSSHPKVIEAAKKAIDDHGYGMSSVRFICGTQDVHKELEAKISKFLGTEDTILYAAAFDANGGVFEPLFNAEDAIISDELNHASIIDGVRLCKAQRFRYKNADMEDLEKQLIAAKDCRHRIIVTDGAFSMDGSVAPLDKIADLADKYEALIMIDESHCTGFIGKTGRGTHEHFDVMDRIDIITGTLGKALGGASGGFTSGKKEIVEMLRQRSRPYLFSNTLAPAIAGASIAVLDMLSETTSLRDKLESNTKYFREKMTEAGFDIKPGFHPIVPVMLYDAKIAQNFAAKMLQEGIYVVGFFYPVVGQGKARIRVQLSAGHEQHHLDKAIAAFTKVGKELGVI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SJCY01000013
EMBL· GenBank· DDBJ
TDG35077.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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