Q8GXU8 · LPAT1_ARATH
- Protein1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- GeneLPAT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids356 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plastidial enzyme of the prokaryotic glycerol-3-phosphate pathway that converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at position sn-2 (PubMed:15169931).
Utilizes palmitoyl-ACP (16:0-ACP) to produce phosphatidic acid containing a saturated group at position sn-2, which is characteristic of lipids synthesized by the prokaryotic pathway (PubMed:15169931).
In vitro, can use 16:0-CoA as acyl donor (PubMed:14976237).
Essential for embryo development during the transition from the globular to the heart stage when chloroplasts begin to form (PubMed:14976237, PubMed:15169931).
Utilizes palmitoyl-ACP (16:0-ACP) to produce phosphatidic acid containing a saturated group at position sn-2, which is characteristic of lipids synthesized by the prokaryotic pathway (PubMed:15169931).
In vitro, can use 16:0-CoA as acyl donor (PubMed:14976237).
Essential for embryo development during the transition from the globular to the heart stage when chloroplasts begin to form (PubMed:14976237, PubMed:15169931).
Catalytic activity
- a fatty acyl-[ACP] + a 1-acyl-sn-glycero-3-phosphate = a 1,2-diacyl-sn-glycero-3-phosphate + holo-[ACP]This reaction proceeds in the forward direction.
Pathway
Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast envelope | |
Cellular Component | chloroplast membrane | |
Cellular Component | plasma membrane | |
Cellular Component | plastid | |
Molecular Function | 1-acylglycerol-3-phosphate O-acyltransferase activity | |
Biological Process | CDP-diacylglycerol biosynthetic process | |
Biological Process | embryo development ending in seed dormancy | |
Biological Process | phosphatidylglycerol biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8GXU8
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Plastid, chloroplast membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 127-147 | Helical | ||||
Sequence: GIFFCVVAGISATFLIVLMII | ||||||
Transmembrane | 224-244 | Helical | ||||
Sequence: TGIFVIPIIGWAMSMMGVVPL |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryonic lethality due to embryo development arrest at globular stage.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 230 | In lpat1-4; suppression of the sensitivity of fab1 mutant plants to low temperature. | ||||
Sequence: P → L | ||||||
Mutagenesis | 290 | In lpat1-3; suppression of the sensitivity of fab1 mutant plants to low temperature. | ||||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-56 | Chloroplast | ||||
Sequence: MDVASARSISSHPSYYGKPICSSQSSLIRISRDKVCCFGRISNGMTSFTTSLHAVP | ||||||
Chain | PRO_0000024701 | 57-356 | 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic | |||
Sequence: SEKFMGETRRTGIQWSNRSLRHDPYRFLDKKSPRSSQLARDITVRADLSGAATPDSSFPEPEIKLSSRLRGIFFCVVAGISATFLIVLMIIGHPFVLLFDPYRRKFHHFIAKLWASISIYPFYKINIEGLENLPSSDTPAVYVSNHQSFLDIYTLLSLGKSFKFISKTGIFVIPIIGWAMSMMGVVPLKRMDPRSQVDCLKRCMELLKKGASVFFFPEGTRSKDGRLGSFKKGAFTVAAKTGVAVVPITLMGTGKIMPTGSEGILNHGNVRVIIHKPIHGSKADVLCNEARSKIAESMDL |
Proteomic databases
Expression
Tissue specificity
Widely expressed. Expressed at higher level in leaves. Expressed at lower level in silique walls compared to leaves.
Developmental stage
Expression transiently increases in siliques 4 hours after flowering.
Gene expression databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 202-207 | HXXXXD motif | ||||
Sequence: HQSFLD |
Domain
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence similarities
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q8GXU8-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length356
- Mass (Da)39,395
- Last updated2003-03-01 v1
- Checksum27A9EB5EBE028940
Q8GXU8-2
- Name2
- Differences from canonical
- 1-144: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_013594 | 1-144 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL161577 EMBL· GenBank· DDBJ | CAB79776.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE85783.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY136460 EMBL· GenBank· DDBJ | AAM97125.1 EMBL· GenBank· DDBJ | mRNA | ||
BT006253 EMBL· GenBank· DDBJ | AAP13361.1 EMBL· GenBank· DDBJ | mRNA | ||
AK118028 EMBL· GenBank· DDBJ | BAC42660.1 EMBL· GenBank· DDBJ | mRNA |