A0A2A3TW02 · A0A2A3TW02_LEVBR
- Proteinthreonine-phosphate decarboxylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids362 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
Function
function
Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
Catalytic activity
- O-phospho-L-threonine + H+ = (R)-1-aminopropan-2-yl phosphate + CO2
Cofactor
Pathway
Cofactor biosynthesis; adenosylcobalamin biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | threonine-phosphate decarboxylase activity | |
Biological Process | cobalamin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namethreonine-phosphate decarboxylase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Levilactobacillus
Accessions
- Primary accessionA0A2A3TW02
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-351 | Aminotransferase class I/classII large | ||||
Sequence: LLDFSANINPLGVPTAARATLVAALDELSDYPNPDYPRLKTAIARHHHVNLADVFVGNGAVQLIFNAALALEVKEALILAPCFGEYERALTKTHAHVNRLYLSADKNFQVDVDELIRRLQHAPSIGLVCLGNPNNPTGTNLNGVAMRQLVNYCNQHQIWLILDEAFMDLTLSAHGSWLPQLTAQDHVLVVRSMTKFFAIPGLRLGYAITKNPELQQRLTWQNEPWSINIVAARFGEQAFKYNTYIRQTQDWLRHEQPWLEQQLNRIPFLKVYPSCTNFFLLKSNRARLREQLWSTGILIRDCSDYEGLTAGYYRVAVKDRAANQQLLQQ |
Family and domain databases
Sequence
- Sequence statusComplete
- Length362
- Mass (Da)41,106
- Last updated2017-12-20 v1
- ChecksumA662450ACE793160