A0A455UBK1 · A0A455UBK1_9GAMM

Function

function

Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.

Catalytic activity

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per monomer. In the dimeric form the Ca2+ is bound by different amino acids with binding of each Ca2+ shared with ligands coming from each monomer. The Ca2+ ion may have a role in catalysis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site169Ca2+ 1 (UniProtKB | ChEBI); in dimeric form
Active site205Proton acceptor
Active site207Nucleophile
Binding site210Ca2+ 1 (UniProtKB | ChEBI); in dimeric form
Binding site215Ca2+ 1 (UniProtKB | ChEBI); in dimeric form
Binding site250Ca2+ 1 (UniProtKB | ChEBI); in dimeric form

GO annotations

AspectTerm
Cellular Componentcell outer membrane
Molecular Function1-acyl-2-lysophosphatidylserine acylhydrolase activity
Molecular Functioncalcium ion binding
Molecular Functionphosphatidylserine 1-acylhydrolase activity
Molecular Functionphospholipase A1 activity
Molecular Functionphospholipase A2 activity
Biological Processlipid catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phospholipase A1
  • EC number
  • Alternative names
    • Phosphatidylcholine 1-acylhydrolase

Gene names

    • ORF names
      HSBAA_42730

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ATCC BAA-803
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Vreelandella

Accessions

  • Primary accession
    A0A455UBK1

Proteomes

Subcellular Location

Cell outer membrane
; Multi-pass membrane protein
Membrane
; Multi-pass membrane protein
Note: One of the very few enzymes located there.

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-26
ChainPRO_501961055827-343Phospholipase A1

Interaction

Subunit

Homodimer; dimerization is reversible, and the dimeric form is the active one.

Family & Domains

Features

Showing features for coiled coil, region, compositional bias.

TypeIDPosition(s)Description
Coiled coil22-49
Region55-90Disordered
Compositional bias69-87Basic and acidic residues

Sequence similarities

Belongs to the phospholipase A1 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    343
  • Mass (Da)
    39,531
  • Last updated
    2019-06-05 v1
  • Checksum
    2EF13941A5A61298
MVTRKLPFTKLIILLSFATFSADAFAASQQEIEERIRALNAELYDLHQQLQRVESPEDAAQGVPFEPLPEEAAREDLSERRELEQESSRNPFSITTHRTNYLFPVSFNANKNRESFRNISGDGEVSSVELKFQFSAKVNLIEEVFGNYGDVYFGYTQRSWWQAYNTDASSPFRETNYEPEVFIDFDNAWGALGWVNTRNRVALNHQSNGRSDPLSRSWNRVYLESTFQRGDWAFTLAPHWRIPESSEDDDNPDIERYMGYGDIRLAKRLNNNHEVSGLLRGNPSAGNIGTQIDYSWPAFNSLRAHVQYYYGYGESMIDYDHRVHRLSLGFSLNPLFSATGLNR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias69-87Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP019514
EMBL· GenBank· DDBJ
BBI62967.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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