Q9LLY4 · LPAT1_BRANA
- Protein1-acyl-sn-glycerol-3-phosphate acyltransferase BAT2, chloroplastic
- GeneBAT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids344 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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:10398728).
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:10398728).
In vitro, can use 16:0-CoA as acyl donor (PubMed:10398728).
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:10398728).
In vitro, can use 16:0-CoA as acyl donor (PubMed:10398728).
Catalytic activity
- a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = 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 membrane | |
Molecular Function | 1-acylglycerol-3-phosphate O-acyltransferase activity | |
Biological Process | CDP-diacylglycerol biosynthetic process | |
Biological Process | phosphatidic acid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name1-acyl-sn-glycerol-3-phosphate acyltransferase BAT2, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica
Accessions
- Primary accessionQ9LLY4
- Secondary accessions
Proteomes
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 | 113-133 | Helical | ||||
Sequence: GICFCLVAGVSAIVLIVLMIT | ||||||
Transmembrane | 210-230 | Helical | ||||
Sequence: TGIFVIPVIGWAMSMMGVVPL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-49 | Chloroplast | ||||
Sequence: MDVASAPGVSSHPPYYSKPICSSQSSLIRIPINKGCCFARSSNLITSLH | ||||||
Chain | PRO_0000024702 | 50-344 | 1-acyl-sn-glycerol-3-phosphate acyltransferase BAT2, chloroplastic | |||
Sequence: AASRGVTRRTSGVQWCYRSIRFDPFKVNDKNSRTVTVRSDLSGAATPESTYPEPEIKLSSRLRGICFCLVAGVSAIVLIVLMITGHPFVLLFDRYRRKFHHFIAKLWASISIYPFYKTDIQGLENLPSSDTPCVYVSNHQSFLDIYTLLSLGQSYKFISKTGIFVIPVIGWAMSMMGVVPLKRMDPRSQVDCLKRCMELVKKGASVFFFPEGTRSKDGRLGPFKKGAFTIAAKTGVPVVPITLMGTGKIMPTGSEGILNHGDVRVIIHKPIYGSKADLLCDEARNKIAESMNLVS |
Proteomic databases
Expression
Tissue specificity
Widely expressed.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 188-193 | 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
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length344
- Mass (Da)37,925
- Last updated2019-07-03 v2
- ChecksumC80E6F32CB7D0627
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 7 | in Ref. 1; AAF73736 and 2; AEE01048 | ||||
Sequence: P → R | ||||||
Sequence conflict | 33 | in Ref. 1; AAF73736 and 2; AEE01048 | ||||
Sequence: N → S | ||||||
Sequence conflict | 122 | in Ref. 1; AAF73736 and 2; AEE01048 | ||||
Sequence: V → I | ||||||
Sequence conflict | 133 | in Ref. 1; AAF73736 and 2; AEE01048 | ||||
Sequence: T → I | ||||||
Sequence conflict | 327-330 | in Ref. 1; AAF73736 and 2; AEE01048 | ||||
Sequence: LLCD → VLCE | ||||||
Sequence conflict | 343 | in Ref. 1; AAF73736 and 2; AEE01048 | ||||
Sequence: V → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF111161 EMBL· GenBank· DDBJ | AAF73736.1 EMBL· GenBank· DDBJ | mRNA | ||
HQ141075 EMBL· GenBank· DDBJ | AEE01048.1 EMBL· GenBank· DDBJ | mRNA | ||
LK032443 EMBL· GenBank· DDBJ | CDY39220.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |