Q9CAY3 · GPAT5_ARATH
- ProteinGlycerol-3-phosphate acyltransferase 5
- GeneGPAT5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids502 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.
Catalytic activity
- an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Kinetics
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
86.85 pmol/min/mg |
Pathway
Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | glycerol-3-phosphate 2-O-acyltransferase activity | |
Molecular Function | glycerol-3-phosphate O-acyltransferase activity | |
Molecular Function | sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity | |
Biological Process | CDP-diacylglycerol biosynthetic process | |
Biological Process | suberin biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol-3-phosphate acyltransferase 5
- EC number
- Short namesAtGPAT5
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9CAY3
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 31-51 | Helical | ||||
Sequence: FMLVAFEAAGLIRFAILLFLW | ||||||
Transmembrane | 237-257 | Helical | ||||
Sequence: ALIILLWIPFGIILAVIRIFL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000195253 | 1-502 | Glycerol-3-phosphate acyltransferase 5 | |||
Sequence: MVMEQAGTTSYSVVSEFEGTILKNADSFSYFMLVAFEAAGLIRFAILLFLWPVITLLDVFSYKNAALKLKIFVATVGLREPEIESVARAVLPKFYMDDVSMDTWRVFSSCKKRVVVTRMPRVMVERFAKEHLRADEVIGTELIVNRFGFVTGLIRETDVDQSALNRVANLFVGRRPQLGLGKPALTASTNFLSLCEEHIHAPIPENYNHGDQQLQLRPLPVIFHDGRLVKRPTPATALIILLWIPFGIILAVIRIFLGAVLPLWATPYVSQIFGGHIIVKGKPPQPPAAGKSGVLFVCTHRTLMDPVVLSYVLGRSIPAVTYSISRLSEILSPIPTVRLTRIRDVDAAKIKQQLSKGDLVVCPEGTTCREPFLLRFSALFAELTDRIVPVAMNYRVGFFHATTARGWKGLDPIFFFMNPRPVYEITFLNQLPMEATCSSGKSPHDVANYVQRILAATLGFECTNFTRKDKYRVLAGNDGTVSYLSLLDQLKKVVSTFEPCLH |
Proteomic databases
Expression
Tissue specificity
Weakly or not expressed in roots, leaves, seedlings, developing siliques and flower buds.
Gene expression databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 300-305 | HXXXXD motif | ||||
Sequence: HRTLMD |
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 GPAT/DAPAT family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length502
- Mass (Da)56,081
- Last updated2001-06-01 v1
- Checksum32E612BD3A21CD6E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC008153 EMBL· GenBank· DDBJ | AAG51432.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE75046.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK117634 EMBL· GenBank· DDBJ | BAC42290.1 EMBL· GenBank· DDBJ | mRNA | ||
BT005134 EMBL· GenBank· DDBJ | AAO50667.1 EMBL· GenBank· DDBJ | mRNA |