A0A1Y0N1Z5 · A0A1Y0N1Z5_9FLAO
- Protein2-amino-3-ketobutyrate coenzyme A ligase
- Genekbl
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids397 (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 | ||||
Sequence: H | ||||||
Binding site | 185 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: S | ||||||
Binding site | 241-244 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: TLGK | ||||||
Binding site | 274-275 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: SN | ||||||
Binding site | 368 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
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 > Flavobacteriia > Flavobacteriales > Flavobacteriaceae
Accessions
- Primary accessionA0A1Y0N1Z5
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 244 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 43-386 | Aminotransferase class I/classII large | ||||
Sequence: EVINFCANNYLGLSNHPEVIQAAKDTMDTHGFGMSSVRFICGTQDIHKQLEKTIANFYTTEDTILYAAAFDANGGVFEPLLTKEDAIISDSLNHASIIDGVRLCKAARYRYNNNDMTSLEEQLIEANKQNHRFKIIVTDGVFSMDGIVAKLDEICDLADKYDALVMVDECHATGFIGKTGRGTVELKNVMDRVDIVTGTLGKALGGAMGGYTTGKKEIIEILRQRSRPYLFSNSLAPGIVGATLKVFDLISDDTSLRDKLEWNTNYFRTEMEKAGFDLVGADAAIVPVMLYDAKLSQVMANKLLEKGIYVIGFFFPVVPKEKARIRVQLSAAHTKDHLNKAITA |
Sequence similarities
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length397
- Mass (Da)43,975
- Last updated2017-08-30 v1
- ChecksumB67BEC9D6438B44F
Keywords
- Technical term