IED ID | IndEnz0004000028 |
Enzyme Type ID | xylanase000028 |
Protein Name |
Glycerol-3-phosphate acyltransferase Acyl-PO4 G3P acyltransferase Acyl-phosphate--glycerol-3-phosphate acyltransferase G3P acyltransferase GPAT EC 2.3.1.275 Lysophosphatidic acid synthase LPA synthase |
Gene Name | plsY yneS BSU18070 |
Organism | Bacillus subtilis (strain 168) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
Enzyme Sequence | MLIALLIILAYLIGSIPSGLIVGKLAKGIDIREHGSGNLGATNAFRTLGVKAGSVVIAGDILKGTLATALPFLMHVDIHPLLAGVFAVLGHVFPIFAKFKGGKAVATSGGVLLFYAPLLFITMVAVFFIFLYLTKFVSLSSMLTGIYTVIYSFFVHDTYLLIVVTLLTIFVIYRHRANIKRIINKTEPKVKWL |
Enzyme Length | 193 |
Uniprot Accession Number | Q45064 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by acyl-CoA. {ECO:0000269|PubMed:17557823}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075, ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:59918; EC=2.3.1.275; |
DNA Binding | |
EC Number | 2.3.1.275 |
Enzyme Function | FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. {ECO:0000269|PubMed:17557823, ECO:0000269|PubMed:17645809, ECO:0000269|PubMed:19282621}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Lipid metabolism; phospholipid metabolism. |
nucleotide Binding | |
Features | Chain (1); Transmembrane (5) |
Keywords | Cell membrane;Lipid biosynthesis;Lipid metabolism;Membrane;Phospholipid biosynthesis;Phospholipid metabolism;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 20,966 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:34075 |
Cross Reference Brenda | 2.3.1.275; |