Reviewed,
UniProtKB/Swiss-Prot Q5WUR6 (SGPL_LEGPL)
Last modified
November 3, 2009.
Version 36.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable sphingosine-1-phosphate lyase Short name=SP-lyase Short name=SPL EC=4.1.2.27 Alternative name(s): Sphingosine-1-phosphate aldolase | ||
| Gene names |
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| Organism | Legionella pneumophila (strain Lens) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 297245 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella |
Protein attributes
| Sequence length | 605 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine By similarity. Possibly implicated in influencing the macrophage autophagy pathway. |
| Catalytic activity | Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Sequence similarities | Belongs to the group II decarboxylase family. Sphingosine-1-phosphate lyase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carboxylic acid metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | carboxy-lyase activity Inferred from electronic annotation. Source: InterPro pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro sphinganine-1-phosphate aldolase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity." Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C. Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], PROBABLE FUNCTION. |
| [2] | "Adaptation of Legionella pneumophila to the host environment: role of protein secretion, effectors and eukaryotic-like proteins." Brueggemann H., Cazalet C., Buchrieser C. Curr. Opin. Microbiol. 9:86-94(2006) [PubMed: 16406773] [Abstract] Cited for: POSSIBLE FUNCTION. |
Cross-references
Sequence databases | |
|---|---|
| CR628337 Genomic DNA. Translation: CAH16342.1. | |
| RefSeq | YP_127437.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5WUR6. |
Genome annotation databases | |
| GeneID | 3116125. |
| GenomeReviews | Gene locus lpl2102 in contig CR628337_GR. |
| KEGG | lpf:lpl2102. |
| NMPDR | fig|297245.3.peg.1227. |
Organism-specific databases | |
| LegioList | lpl2102. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q5WUR6. |
| OMA | AEREDRN. |
Enzyme and pathway databases | |
| BioCyc | LPNE297245:LPL2102-MON. |
Family and domain databases | |
| InterPro | IPR002129. PyrdxlP-dep_de-COase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. |
| PANTHER | PTHR11999. Pyridoxal_deC. 1 hit. |
| Pfam | PF00282. Pyridoxal_deC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SGPL_LEGPL | ||||||||
| Accession | Primary (citable) accession number: Q5WUR6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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