Reviewed,
UniProtKB/Swiss-Prot B7MJ31 (PLSB_ECO45)
Last modified
October 13, 2009.
Version 7.
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 Short name=GPAT EC=2.3.1.15 | ||||
| Gene names |
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| Organism | Escherichia coli O45:K1 (strain S88 / ExPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 585035 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 807 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. HAMAP MF_00393 |
| Pathway | Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. HAMAP MF_00393 |
| Subcellular location | Cell membrane; Peripheral membrane protein By similarity. |
| 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 | Cell membrane Membrane |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phospholipid biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: HAMAP |
| Molecular function | glycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 807 | 807 | Glycerol-3-phosphate acyltransferase HAMAP MF_00393 | PRO_1000123075 | |||||
Regions | |||||||||
| Motif | 305 – 310 | 6 | HXXXXD motif HAMAP MF_00393 | ||||||
Sequences
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References
| [1] | "Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. Denamur E.PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CU928161 Genomic DNA. Translation: CAR05675.1. | |
| RefSeq | YP_002394024.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 7130380. |
| GenomeReviews | Gene locus ECS88_4514 in contig CU928161_GR. |
Organism-specific databases | |
| CMR | Search... |
Family and domain databases | |
| HAMAP | MF_00393. [Tree] |
| InterPro | IPR002123. Acyltransferase. [Graphical view] |
| Pfam | PF01553. Acyltransferase. 1 hit. [Graphical view] |
| SMART | SM00563. PlsC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PLSB_ECO45 | ||||||||
| Accession | Primary (citable) accession number: B7MJ31 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


