Detail Information for IndEnz0005001068
IED ID IndEnz0005001068
Enzyme Type ID lipase001068
Protein Name 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
EC 2.3.1.51
Abhydrolase domain-containing protein 5
Gene Name ABHD5
Organism Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Enzyme Sequence MAAEEEEVDSADTGERSGWLTGWLPTWCPTSTSHLKEAEEKMLKCVPCTYKKEPVHISNGNKIWTLKFSHNISNKTPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLADQDRPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGKMHPDIPVSVIFGARSCIDGNSGTSIQSLRPHSYVKTIAILGAGHYVYADQPEEFNQKVKEICDTVD
Enzyme Length 349
Uniprot Accession Number Q5RBI4
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Acyltransferase activity is inhibited by detergents such as Triton X-100 and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Acyltransferase activity is inhibited by the presence of magnesium and calcium. {ECO:0000250|UniProtKB:Q9DBL9}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; Evidence={ECO:0000250|UniProtKB:Q8WTS1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710; Evidence={ECO:0000250|UniProtKB:Q8WTS1}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74544, ChEBI:CHEBI:74546; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74544, ChEBI:CHEBI:74551; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:74544, ChEBI:CHEBI:74552; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544, ChEBI:CHEBI:74928; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA = 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37451, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:74544, ChEBI:CHEBI:74937; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37452; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57518, ChEBI:CHEBI:64839; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74560, ChEBI:CHEBI:74565; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164; Evidence={ECO:0000250|UniProtKB:Q9DBL9}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37455, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74938, ChEBI:CHEBI:74941; Evidence={ECO:0000250|UniProtKB:Q9DBL9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456; Evidence={ECO:0000250|UniProtKB:Q9DBL9};
DNA Binding
EC Number 2.3.1.51
Enzyme Function FUNCTION: Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (By similarity). Functions in phosphatidic acid biosynthesis (By similarity). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (By similarity). Involved in keratinocyte differentiation (By similarity). Regulates lipid droplet fusion (By similarity). {ECO:0000250|UniProtKB:Q8WTS1, ECO:0000250|UniProtKB:Q9DBL9}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Motif (1)
Keywords Acetylation;Acyltransferase;Cytoplasm;Differentiation;Fatty acid metabolism;Lipid biosynthesis;Lipid droplet;Lipid metabolism;Phospholipid biosynthesis;Phospholipid metabolism;Phosphoprotein;Reference proteome;Transferase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Lipid droplet {ECO:0000250}. Note=Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA (By similarity). {ECO:0000250}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q8WTS1; MOD_RES 122; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q6QA69
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 327..332; /note=HXXXXD motif
Gene Encoded By
Mass 39,065
Kinetics
Metal Binding
Rhea ID RHEA:19709; RHEA:19710; RHEA:37131; RHEA:37132; RHEA:37143; RHEA:37144; RHEA:37147; RHEA:37148; RHEA:37443; RHEA:37444; RHEA:37451; RHEA:37452; RHEA:33187; RHEA:33188; RHEA:37163; RHEA:37164; RHEA:37455; RHEA:37456
Cross Reference Brenda