Reviewed,
UniProtKB/Swiss-Prot Q59601 (PLSC_NEIGO)
Last modified
October 13, 2009.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 1-acyl-sn-glycerol-3-phosphate acyltransferase Short name=1-AGP acyltransferase Short name=1-AGPAT EC=2.3.1.51 Alternative name(s): Lysophosphatidic acid acyltransferase Short name=LPAAT | ||
| Gene names |
| ||
| Organism | Neisseria gonorrhoeae | ||
| Taxonomic identifier | 485 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 255 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. |
| Catalytic activity | Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-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 1-acyl-sn-glycerol-3-phosphate acyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phospholipid biosynthesis |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Molecular function | Acyltransferase Transferase |
| Gene Ontology (GO) | |
| Biological process | phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Membrane glycerophospholipid biosynthesis in Neisseria meningitidis and Neisseria gonorrhoeae: identification, characterization, and mutagenesis of a lysophosphatidic acid acyltransferase." Swartley J.S., Balthazar J.T., Coleman J., Shafer W.M., Stephens D.S. Mol. Microbiol. 18:401-412(1995) [PubMed: 8748025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FA19. |
Cross-references
Sequence databases | |
|---|---|
| U21806 Genomic DNA. Translation: AAB40877.1. | |
| PIR | S70545. |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.51. 588. |
Family and domain databases | |
| InterPro | IPR002123. Acyltransferase. IPR004552. AGP_acyltrans. [Graphical view] |
| Pfam | PF01553. Acyltransferase. 1 hit. [Graphical view] |
| SMART | SM00563. PlsC. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00530. AGP_acyltrn. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PLSC_NEIGO | ||||||||
| Accession | Primary (citable) accession number: Q59601 | ||||||||
| 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


