A0A4R5MHP1 · A0A4R5MHP1_9SPHI
- Protein2-amino-3-ketobutyrate coenzyme A ligase
- Genekbl
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids395 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
Catalytic activity
- glycine + acetyl-CoA = (2S)-2-amino-3-oxobutanoate + CoA
Cofactor
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 136 | substrate | |||
Binding site | 183 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 208-211 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 239-242 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 272-273 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 366 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | glycine C-acetyltransferase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | biosynthetic process | |
Biological Process | L-threonine catabolic process to glycine |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-amino-3-ketobutyrate coenzyme A ligase
- EC number
- Short namesAKB ligase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Pedobacter
Accessions
- Primary accessionA0A4R5MHP1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 242 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 43-384 | Aminotransferase class I/classII large | |||
Sequence similarities
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length395
- Mass (Da)43,325
- Last updated2019-07-31 v1
- MD5 Checksum25965375C4639DA7170F7EE67A8B4A8C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SJCY01000013 EMBL· GenBank· DDBJ | TDG35077.1 EMBL· GenBank· DDBJ | Genomic DNA |