Detail Information for IndEnz0005000045
IED ID IndEnz0005000045
Enzyme Type ID lipase000045
Protein Name Phospholipid:diacylglycerol acyltransferase
PDAT
EC 2.3.1.158
Pombe LRO1 homolog 1
Triacylglycerol synthase
TAG synthase
Gene Name plh1 SPBC776.14
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Enzyme Sequence MASSKKSKTHKKKKEVKSPIDLPNSKKPTRALSEQPSASETQSVSNKSRKSKFGKRLNFILGAILGICGAFFFAVGDDNAVFDPATLDKFGNMLGSSDLFDDIKGYLSYNVFKDAPFTTDKPSQSPSGNEVQVGLDMYNEGYRSDHPVIMVPGVISSGLESWSFNNCSIPYFRKRLWGSWSMLKAMFLDKQCWLEHLMLDKKTGLDPKGIKLRAAQGFEAADFFITGYWIWSKVIENLAAIGYEPNNMLSASYDWRLSYANLEERDKYFSKLKMFIEYSNIVHKKKVVLISHSMGSQVTYYFFKWVEAEGYGNGGPTWVNDHIEAFINISGSLIGAPKTVAALLSGEMKDTAQLNQFSVYGLEKFFSRSERAMMVRTMGGVSSMLPKGGDVVWGNASWAPDDLNQTNFSNGAIIRYREDIDKDHDEFDIDDALQFLKNVTDDDFKVMLAKNYSHGLAWTEKEVLKNNEMPSKWINPLETSLPYAPDMKIYCVHGVGKPTERGYYYTNNPEGQPVIDSSVNDGTKVENGIVMDDGDGTLPILALGLVCNKVWQTKRFNPANTSITNYEIKHEPAAFDLRGGPRSAEHVDILGHSELNEIILKVSSGHGDSVPNRYISDIQEIINEINLDKPRN
Enzyme Length 632
Uniprot Accession Number O94680
Absorption
Active Site ACT_SITE 293; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q8NCC3; ACT_SITE 535; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q8NCC3; ACT_SITE 586; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q8NCC3
Activity Regulation
Binding Site BINDING 136; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NCC3; BINDING 294; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NCC3
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + a glycerophospholipid = a monoacylglycerophospholipid + a triacyl-sn-glycerol; Xref=Rhea:RHEA:14057, ChEBI:CHEBI:17815, ChEBI:CHEBI:64615, ChEBI:CHEBI:136912, ChEBI:CHEBI:136913; EC=2.3.1.158; Evidence={ECO:0000269|PubMed:12963726};
DNA Binding
EC Number 2.3.1.158
Enzyme Function FUNCTION: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA independent pathway. The enzyme specifically transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol (DAG), thus forming an sn-1-lysophospholipid. Plays a major role in triacylglycerol formation at log phase (PubMed:12963726, PubMed:26990381). Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains (PubMed:26990381, PubMed:28011631). {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:26990381, ECO:0000269|PubMed:28011631}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis. {ECO:0000305|PubMed:12963726}.
nucleotide Binding
Features Active site (3); Binding site (2); Chain (1); Compositional bias (1); Region (1); Topological domain (2); Transmembrane (1)
Keywords Acyltransferase;Endoplasmic reticulum;Membrane;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000255}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 20473289; 22633491; 23697806; 30726745; 34250083;
Motif
Gene Encoded By
Mass 70,833
Kinetics
Metal Binding
Rhea ID RHEA:14057
Cross Reference Brenda