Reviewed,
UniProtKB/Swiss-Prot Q43822 (PLSB_PHAVU)
Last modified
February 9, 2010.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glycerol-3-phosphate acyltransferase, chloroplastic Short name=GPAT EC=2.3.1.15 | ||
| Gene names |
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| Organism | Phaseolus vulgaris (Kidney bean) (French bean) | ||
| Taxonomic identifier | 3885 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Phaseolus |
Protein attributes
| Sequence length | 461 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate. The enzyme from chilling-resistant plants discriminates against non-fluid palmitic acid and selects oleic acid whereas the enzyme from sensitive plants accepts both fatty acids. |
| Catalytic activity | Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. |
| Pathway | |
| Subcellular location | |
| Domain | The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity. |
| Sequence similarities | Belongs to the GPAT/DAPAT family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phospholipid biosynthesis |
| Cellular component | Chloroplast Plastid |
| Domain | Transit peptide |
| Molecular function | Acyltransferase Transferase |
| Gene Ontology (GO) | |
| Biological process | phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | glycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Cloning and sequencing of a full-length cDNA coding for sn-glycerol-3-phosphate acyltransferase from Phaseolus vulgaris." Fritz M., Heinz E., Wolter F.P. Plant Physiol. 107:1039-1040(1995) [PubMed: 7716242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Annabel. Tissue: Leaf. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X79722 mRNA. Translation: CAA56159.1. |
| PIR | T11819. |
3D structure databases | |
| SMR | Q43822. Positions 97-460. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.15. 8. |
Family and domain databases | |
| InterPro | IPR002123. Acyltransferase. IPR016222. Glycerol-3-P_O-acyltransferase. [Graphical view] |
| Pfam | PF01553. Acyltransferase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000431. Glycerol-3-P_O-acyltransfrase. 1 hit. |
| SMART | SM00563. PlsC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PLSB_PHAVU | ||||||||
| Accession | Primary (citable) accession number: Q43822 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


