Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT; ...
200-435
9.09e-127
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT; Lysophospholipid acyltransferase (LPLAT) superfamily member: glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB). LPLATs are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. This subgroup includes glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB).
Pssm-ID: 153247 Cd Length: 235 Bit Score: 367.15 E-value: 9.09e-127
Glycerol-3-phosphate acyltransferase N-terminal; GPAT_N is the N-terminal domain of ...
95-170
3.73e-44
Glycerol-3-phosphate acyltransferase N-terminal; GPAT_N is the N-terminal domain of glycerol-3-phosphate acyltransferases, and it forms a four-helix bundle. Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the incorporation of an acyl group from either acyl-acyl carrier proteins or acyl-CoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol-3-phosphate. G3PATs can either be selective, preferentially using the unsaturated fatty acid, oleate (C18:1), as the acyl donor, or non-selective, using either oleate or the saturated fatty acid, palmitate (C16:0), at comparable rates. The differential substrate-specificity for saturated versus unsaturated fatty acids seen within this enzyme family has been implicated in the sensitivity of plants to chilling temperatures. The exact function of this domain is not known. it lies upstream of family Acyltransferase, pfam01553.
Pssm-ID: 373324 Cd Length: 76 Bit Score: 149.06 E-value: 3.73e-44
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
223-328
6.90e-08
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.
Pssm-ID: 214724 [Multi-domain] Cd Length: 118 Bit Score: 50.82 E-value: 6.90e-08
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
186-384
5.23e-07
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 439974 [Multi-domain] Cd Length: 215 Bit Score: 50.39 E-value: 5.23e-07
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT; ...
200-435
9.09e-127
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT; Lysophospholipid acyltransferase (LPLAT) superfamily member: glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB). LPLATs are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. This subgroup includes glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB).
Pssm-ID: 153247 Cd Length: 235 Bit Score: 367.15 E-value: 9.09e-127
Glycerol-3-phosphate acyltransferase N-terminal; GPAT_N is the N-terminal domain of ...
95-170
3.73e-44
Glycerol-3-phosphate acyltransferase N-terminal; GPAT_N is the N-terminal domain of glycerol-3-phosphate acyltransferases, and it forms a four-helix bundle. Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the incorporation of an acyl group from either acyl-acyl carrier proteins or acyl-CoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol-3-phosphate. G3PATs can either be selective, preferentially using the unsaturated fatty acid, oleate (C18:1), as the acyl donor, or non-selective, using either oleate or the saturated fatty acid, palmitate (C16:0), at comparable rates. The differential substrate-specificity for saturated versus unsaturated fatty acids seen within this enzyme family has been implicated in the sensitivity of plants to chilling temperatures. The exact function of this domain is not known. it lies upstream of family Acyltransferase, pfam01553.
Pssm-ID: 373324 Cd Length: 76 Bit Score: 149.06 E-value: 3.73e-44
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
209-366
9.49e-19
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.
Pssm-ID: 366704 [Multi-domain] Cd Length: 131 Bit Score: 81.94 E-value: 9.49e-19
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
212-425
2.00e-13
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).
Pssm-ID: 153244 [Multi-domain] Cd Length: 187 Bit Score: 68.59 E-value: 2.00e-13
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
223-328
6.90e-08
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.
Pssm-ID: 214724 [Multi-domain] Cd Length: 118 Bit Score: 50.82 E-value: 6.90e-08
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
186-384
5.23e-07
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 439974 [Multi-domain] Cd Length: 215 Bit Score: 50.39 E-value: 5.23e-07
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
215-384
6.71e-06
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.
Pssm-ID: 153251 [Multi-domain] Cd Length: 184 Bit Score: 46.50 E-value: 6.71e-06
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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