P19265 · EUTC_SALTY

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).
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

Cofactor

adenosylcob(III)alamin (UniProtKB | Rhea| CHEBI:18408 )

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 μMadenosylcob(III)alamin

Pathway

Amine and polyamine degradation; ethanolamine degradation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site210adenosylcob(III)alamin (UniProtKB | ChEBI)
Binding site231adenosylcob(III)alamin (UniProtKB | ChEBI)
Binding site261adenosylcob(III)alamin (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentethanolamine ammonia-lyase complex
Cellular Componentethanolamine degradation polyhedral organelle
Molecular Functioncobalamin binding
Molecular Functionethanolamine ammonia-lyase activity
Biological Processamino acid metabolic process
Biological Processethanolamine catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ethanolamine ammonia-lyase small subunit
  • EC number
  • Short names
    EAL small subunit
  • Alternative names
    • Ethanolamine ammonia-lyase beta subunit

Gene names

    • Name
      eutC
    • Ordered locus names
      STM2457

Organism names

Accessions

  • Primary accession
    P19265
  • Secondary accessions
    • Q9ZFV0

Proteomes

Subcellular Location

Bacterial microcompartment
Note: Probably located inside the BMC (Probable). Has been suggested to be on the BMC exterior.

Keywords

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).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002060031-298Ethanolamine ammonia-lyase small subunit

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).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-19Targets protein to the BMC

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 status
    Complete
  • Length
    298
  • Mass (Da)
    32,137
  • Last updated
    2000-05-30 v3
  • Checksum
    C681A995C6A1671A
MDQKQIEEIVRSVMASMGQDVPQPAAPSTQEGAKPQCAAPTVTESCALDLGSAEAKAWIGVENPHRADVLTELRRSTAARVCTGRAGPRPRTQALLRFLADHSRSKDTVLKEVPEEWVKAQGLLEVRSEISDKNLYLTRPDMGRRLSPEAIDALKSQCVMNPDVQVVVSDGLSTDAITANYEEILPPLLAGLKQAGLNVGTPFFVRYGRVKIEDQIGEILGAKVVILLVGERPGLGQSESLSCYAVYSPRVATTVEADRTCISNIHQGGTPPVEAAAVIVDLAKRMLEQKASGINMTR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict45in Ref. 1; AAA27062
Sequence conflict82-97in Ref. 1; AAA27062
Sequence conflict122in Ref. 1; AAA27062
Sequence conflict253-298in Ref. 1; AAA27062

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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