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Reviewed, UniProtKB/Swiss-Prot Q5WUR6 (SGPL_LEGPL)

Last modified November 3, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
Ordered Locus Names: lpl2102
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Probable sphingosine-1-phosphate lyase
PRO_0000248942

Amino acid modifications

Modified residue3601N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WUR6-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9D75A08557921015

FASTA60566,495
        10         20         30         40         50         60 
MFGFISDLLT AAVSSLDELL QDTPAHQIIL GTAALYFLYN QYHNPSISRW YLSRNNASMK 

        70         80         90        100        110        120 
QRIIDSAYAL AKNLPGVNQI IEKELNKELS STREKLRIQR SGMTLREEIP EEGLSPQDIL 

       130        140        150        160        170        180 
SAFDVDVEKC HFDFLSVNND SPEREFLVGG GDGKDSGALY AIHPKELTEL LKEVYGATAL 

       190        200        210        220        230        240 
TNPLHDKWPR INAMQAEVIR WCQNLFHGSK EGYGLLTHGG TTSIIEAMAA YVIRARAKGI 

       250        260        270        280        290        300 
DYPEIVVPET AHAAFKKAAE LTGAILITVP VDKKTGAVNP RVMSSYITRN TAVIVGSAPS 

       310        320        330        340        350        360 
FMNGIHDPVS ELGQLAKKKN VPFHVDACLG GFLTAFLDTS SEPMDFRVPG VTSISADLHK 

       370        380        390        400        410        420 
YGCCPKGTSV CLFSEDSPAL SVYAALNWSG GLYATPGILD GSTSGARVAE VYATLSYYGK 

       430        440        450        460        470        480 
NKYQEIAKSI IKLRNAIQKE LTALVEEGNG LTSEDIYVYG NPQWSILGFR SNTCNAHFIA 

       490        500        510        520        530        540 
DELEKRGWKL NLLQNPDGFH LCLTHVHTLV RGFETQFIKD LREAVIDVKN YPPGKKASGN 

       550        560        570        580        590        600 
VKVYGAVGMM PIELQKEICK QYQKARLDFT AASHGSLGIF TTSPTEEDDG LRNRKVGEQK 


VQTSL 

« Hide

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.
RefSeqYP_127437.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WUR6.

Genome annotation databases

GeneID3116125.
GenomeReviewsGene locus lpl2102 in contig CR628337_GR.
KEGGlpf:lpl2102.
NMPDRfig|297245.3.peg.1227.

Organism-specific databases

LegioListlpl2102.
CMRSearch...

Phylogenomic databases

HOGENOMQ5WUR6.
OMAAEREDRN.

Enzyme and pathway databases

BioCycLPNE297245:LPL2102-MON.

Family and domain databases

InterProIPR002129. PyrdxlP-dep_de-COase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11999. Pyridoxal_deC. 1 hit.
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSGPL_LEGPL
AccessionPrimary (citable) accession number: Q5WUR6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: November 23, 2004
Last modified: November 3, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents