D5B9D8 · D5B9D8_ZUNPS
- ProteinEthanolamine ammonia-lyase large subunit
- GeneeutB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids456 (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 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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 160-162 | substrate | |||
Binding site | 193 | substrate | |||
Binding site | 194 | adenosylcob(III)alamin (UniProtKB | ChEBI) | |||
Binding site | 245 | adenosylcob(III)alamin (UniProtKB | ChEBI) | |||
Binding site | 287 | substrate | |||
Binding site | 295 | adenosylcob(III)alamin (UniProtKB | ChEBI) | |||
Binding site | 362 | substrate | |||
Binding site | 401 | adenosylcob(III)alamin (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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 large subunit
- EC number
- Short namesEAL large subunit
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Zunongwangia
Accessions
- Primary accessionD5B9D8
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.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length456
- Mass (Da)50,589
- Last updated2010-06-15 v1
- MD5 Checksum0BCCE35FD0A83662B40078FBB5C38E62
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001650 EMBL· GenBank· DDBJ | ADF52223.1 EMBL· GenBank· DDBJ | Genomic DNA |