P19265 · EUTC_SALTY
- ProteinEthanolamine ammonia-lyase small subunit
- GeneeutC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids298 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds (Probable). It is spontaneously inactivated by its substrate and reactivated by EutA (By similarity).
May play a role in bacterial microcompartment (BMC) assembly or maintenance (Probable). Directly targeted to the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681).
May play a role in bacterial microcompartment (BMC) assembly or maintenance (Probable). Directly targeted to the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681).
Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase activity and to induce the operon. EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136).
Catalytic activity
- ethanolamine = acetaldehyde + NH4+
Cofactor
Note: Binds between the large and small subunits.
Biotechnology
Artificial BMCs can be made in E.coli by expressing eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins can be targeted to them using the first 19 residues of this protein. Beta-galactosidase (lacZ) was active within the BMC, showing the BMC allows passage of substrate into the interior. This can lead to the development of tailored BMCs for specific metabolic reactions.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.51 μM | adenosylcob(III)alamin |
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
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEthanolamine ammonia-lyase small subunit
- EC number
- Short namesEAL small subunit
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionP19265
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Probably located inside the BMC (Probable). Has been suggested to be on the BMC exterior.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203, PubMed:2656649).
A non-polar deletion mutant does not grow on EA between pH 5.5 and pH 8.5 (PubMed:16585748).
A deletion allows growth on acetate, suggesting BMC assembly or maintenance is impaired (PubMed:23585538).
A non-polar deletion mutant does not grow on EA between pH 5.5 and pH 8.5 (PubMed:16585748).
A deletion allows growth on acetate, suggesting BMC assembly or maintenance is impaired (PubMed:23585538).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000206003 | 1-298 | Ethanolamine ammonia-lyase small subunit | |||
Sequence: MDQKQIEEIVRSVMASMGQDVPQPAAPSTQEGAKPQCAAPTVTESCALDLGSAEAKAWIGVENPHRADVLTELRRSTAARVCTGRAGPRPRTQALLRFLADHSRSKDTVLKEVPEEWVKAQGLLEVRSEISDKNLYLTRPDMGRRLSPEAIDALKSQCVMNPDVQVVVSDGLSTDAITANYEEILPPLLAGLKQAGLNVGTPFFVRYGRVKIEDQIGEILGAKVVILLVGERPGLGQSESLSCYAVYSPRVATTVEADRTCISNIHQGGTPPVEAAAVIVDLAKRMLEQKASGINMTR |
Proteomic databases
Expression
Induction
Part of the 17-gene eut operon transcribed from a single promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl, vitamin B12).
Interaction
Subunit
The basic unit is a heterodimer which dimerizes to form tetramers (PubMed:1550360).
The heterotetramers trimerize; 6 large subunits form a core ring with 6 small subunits projecting outwards (Probable). Interacts with EutS, which targets it to the interior of the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681).
The heterotetramers trimerize; 6 large subunits form a core ring with 6 small subunits projecting outwards (Probable). Interacts with EutS, which targets it to the interior of the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-19 | Targets protein to the BMC | ||||
Sequence: MDQKQIEEIVRSVMASMGQ |
Domain
The first 19 residues target foreign proteins (tested with eGFP, mCherry and lacZ) to the BMC both in situ and in E.coli. The cargo is only detected by Western blot in broken shells, strongly suggesting this protein is normally found inside the BMC and not on its exterior.
Sequence similarities
Belongs to the EutC family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length298
- Mass (Da)32,137
- Last updated2000-05-30 v3
- ChecksumC681A995C6A1671A
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 45 | in Ref. 1; AAA27062 | ||||
Sequence: S → T | ||||||
Sequence conflict | 82-97 | in Ref. 1; AAA27062 | ||||
Sequence: CTGRAGPRPRTQALLR → LYGACRAASAHPGAVA | ||||||
Sequence conflict | 122 | in Ref. 1; AAA27062 | ||||
Sequence: G → GLLEVRSEEWVKAQG | ||||||
Sequence conflict | 253-298 | in Ref. 1; AAA27062 | ||||
Sequence: TTVEADRTCISNIHQGGTPPVEAAAVIVDLAKRMLEQKASGINMTR → PPSRPTEPVFQTFIRGGRRQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J05518 EMBL· GenBank· DDBJ | AAA27062.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF093749 EMBL· GenBank· DDBJ | AAC78124.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006468 EMBL· GenBank· DDBJ | AAL21351.1 EMBL· GenBank· DDBJ | Genomic DNA |