Detail Information for IndEnz0004000028
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;