P26647 · PLSC_ECOLI

  • Protein
    1-acyl-sn-glycerol-3-phosphate acyltransferase
  • Gene
    plsC
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the 2 position. This enzyme can utilize either acyl-CoA or acyl-ACP as the fatty acyl donor.

Catalytic activity

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Function1-acylglycerol-3-phosphate O-acyltransferase activity
Biological ProcessCDP-diacylglycerol biosynthetic process
Biological Processphosphatidic acid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    1-acyl-sn-glycerol-3-phosphate acyltransferase
  • EC number
  • Short names
    1-AGP acyltransferase; 1-AGPAT
  • Alternative names
    • Lysophosphatidic acid acyltransferase (LPAAT)
    • Phosphatidic acid synthase (PA synthase)

Gene names

    • Name
      plsC
    • Synonyms
      parF
    • Ordered locus names
      b3018, JW2986

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P26647
  • Secondary accessions
    • Q2M9I2

Proteomes

Subcellular Location

Cell inner membrane
; Peripheral membrane protein

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-formylmethionine
ChainPRO_00002081681-2451-acyl-sn-glycerol-3-phosphate acyltransferase

Keywords

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif73-78HXXXXD motif

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    245
  • Mass (Da)
    27,453
  • Last updated
    1992-08-01 v1
  • Checksum
    E9A1E697E7149838
MLYIFRLIITVIYSILVCVFGSIYCLFSPRNPKHVATFGHMFGRLAPLFGLKVECRKPTDAESYGNAIYIANHQNNYDMVTASNIVQPPTVTVGKKSLLWIPFFGQLYWLTGNLLIDRNNRTKAHGTIAEVVNHFKKRRISIWMFPEGTRSRGRGLLPFKTGAFHAAIAAGVPIIPVCVSTTSNKINLNRLHNGLVIVEMLPPIDVSQYGKDQVRELAAHCRSIMEQKIAELDKEVAEREAAGKV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M63491
EMBL· GenBank· DDBJ
AAA24397.1
EMBL· GenBank· DDBJ
Genomic DNA
U28377
EMBL· GenBank· DDBJ
AAA69186.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76054.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77074.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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