P26647 · PLSC_ECOLI
- Protein1-acyl-sn-glycerol-3-phosphate acyltransferase
- GeneplsC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids245 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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
- a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Pathway
Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | 1-acylglycerol-3-phosphate O-acyltransferase activity | |
Biological Process | CDP-diacylglycerol biosynthetic process | |
Biological Process | phosphatidic acid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name1-acyl-sn-glycerol-3-phosphate acyltransferase
- EC number
- Short names1-AGP acyltransferase; 1-AGPAT
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP26647
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-formylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000208168 | 1-245 | 1-acyl-sn-glycerol-3-phosphate acyltransferase | |||
Sequence: MLYIFRLIITVIYSILVCVFGSIYCLFSPRNPKHVATFGHMFGRLAPLFGLKVECRKPTDAESYGNAIYIANHQNNYDMVTASNIVQPPTVTVGKKSLLWIPFFGQLYWLTGNLLIDRNNRTKAHGTIAEVVNHFKKRRISIWMFPEGTRSRGRGLLPFKTGAFHAAIAAGVPIIPVCVSTTSNKINLNRLHNGLVIVEMLPPIDVSQYGKDQVRELAAHCRSIMEQKIAELDKEVAEREAAGKV |
Keywords
- PTM
Proteomic databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 73-78 | HXXXXD motif | ||||
Sequence: HQNNYD |
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
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length245
- Mass (Da)27,453
- Last updated1992-08-01 v1
- ChecksumE9A1E697E7149838
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |