A0A3P6M263 · A0A3P6M263_SHIDY
- ProteinEthanolamine ammonia-lyase small subunit
- GeneeutC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids258 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Catalytic activity
- ethanolamine = acetaldehyde + NH4+
Cofactor
Note: Binds between the large and small subunits.
Pathway
Amine and polyamine degradation; ethanolamine degradation.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | ethanolamine ammonia-lyase complex | |
Cellular Component | ethanolamine degradation polyhedral organelle | |
Molecular Function | cobalamin binding | |
Molecular Function | ethanolamine ammonia-lyase activity | |
Biological Process | amino acid metabolic process | |
Biological Process | ethanolamine catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEthanolamine ammonia-lyase small subunit
- EC number
- Short namesEAL small subunit
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Shigella
Accessions
- Primary accessionA0A3P6M263
Proteomes
Subcellular Location
Interaction
Subunit
The basic unit is a heterodimer which dimerizes to form tetramers. The heterotetramers trimerize; 6 large subunits form a core ring with 6 small subunits projecting outwards.
Structure
Sequence
- Sequence statusComplete
- Length258
- Mass (Da)27,995
- Last updated2019-02-13 v1
- Checksum0FF875BD93DB4A79