A0A0K3Y3G6 · A0A0K3Y3G6_ECOLX

  • Protein
    Ethanolamine ammonia-lyase large subunit
  • Gene
    eutB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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

Cofactor

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

Note: Binds between the large and small subunits.

Pathway

Amine and polyamine degradation; ethanolamine degradation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site160-162substrate
Binding site193substrate
Binding site194adenosylcob(III)alamin (UniProtKB | ChEBI)
Binding site246adenosylcob(III)alamin (UniProtKB | ChEBI)
Binding site287substrate
Binding site295adenosylcob(III)alamin (UniProtKB | ChEBI)
Binding site362substrate
Binding site401adenosylcob(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 large subunit
  • EC number
  • Short names
    EAL large subunit

Gene names

    • Name
      eutB
    • ORF names
      FIJ20_13450
      , TUM18780_12540

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • FSIS11921886
    • TUM18780
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A0K3Y3G6

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.

Family & Domains

Sequence similarities

Belongs to the EutB family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    453
  • Mass (Da)
    49,419
  • Last updated
    2015-11-11 v1
  • Checksum
    B9F7960E089E607E
MKLKTTLFGNVYQFKDVKEVLAKANELRSGDVLAGVAAASSQERVAAKQVLSEMTVADIRNNPVIAYEDDCVTRLIQDDVNETAYNQIKNWSISELREYVLSDETSVDDIAFTRKGLTSEVVAAVAKICSNADLIYGAKKMPVIKKANTTIGIPGTFSARLQPNDTRDDVQSIAAQIYEGLSFGVGDAVIGVNPVTDDVENLSRVLDTIYGVIDKFNIPTQGCVLAHVTTQIEAIRRGAPGGLIFQSICGSEKGLKEFGVELAMLDEARAVGAEFNRIAGENCLYFETGQGSALSAGANYGADQVTMEARNYGLARHYDPFIVNTVVGFIGPEYLYNDRQIIRAGLEDHFMGKLSGISMGCDCCYTNHADADQNLNENLMILLATAGCNYIMGMPLGDDIMLNYQTTAFHDTATVRQLLNLRPSPEFERWLESMGIMANGRLTKRAGDPSLFF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP023197
EMBL· GenBank· DDBJ
BCG36092.1
EMBL· GenBank· DDBJ
Genomic DNA
AASDFP010000026
EMBL· GenBank· DDBJ
EFB2193230.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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