Q5X3A8 (SGPL_LEGPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable sphingosine-1-phosphate lyase
Short name=S1PL
Short name=SP-lyase
Short name=SPL
EC=4.1.2.27

Alternative name(s):
Sphingosine-1-phosphate aldolase

Gene names

Ordered Locus Names:

lpp2128

Organism

Legionella pneumophila (strain Paris) [Complete proteome] [HAMAP]

Taxonomic identifier

297246 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	605 AA.
Sequence status	Complete.
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. Ref.1 Ref.2
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 binding Inferred from electronic annotation. Source: InterPro sphinganine-1-phosphate aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 605	605	Probable sphingosine-1-phosphate lyase		PRO_0000248940
Amino acid modifications
	Modified residue	360	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5X3A8 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 5EEA8D767A4E38C3	FASTA	605	66,481
	10 20 30 40 50 60 MFGFISDLLT AAVSSLDELL QDTPAHQIIL GTAALYFLYN QYHNPSISRW CRSRNNASMK 70 80 90 100 110 120 QRIIDSAYAL AKNLPGVNQI IEKELNKELS STREKLRIQR SGMTLREEIP EEGLSPQDIL 130 140 150 160 170 180 SAFDVDVEKC HFDFLSVTND SPEREFLVGR 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 NVMSSYITRN TAVMVGSAPS 310 320 330 340 350 360 FMNGIHDPIS ELGQLAKKKN VPFHVDACLG GFLTAFLDTS SEPMDFRVPG VTSISADLHK 370 380 390 400 410 420 YGCCPKGTSV CLFSEDSPAL SVYAALNWSG GLYATPGILD GSTSGARVAE VYATLSYYGK 430 440 450 460 470 480 NKYQEIAKSI IRLRNAIQKE LTALVEEGNG LTSEDIYVYG NPQWSILGFR SNTCNAHFIA 490 500 510 520 530 540 DELEKRGWKL NLLQNPDGFH LCLTHVHTLV GSFETQFIKD LREAVIDVKN YPPGKKPSGN 550 560 570 580 590 600 VKVYGAVGMM PVELQKEICK QYQKARLDFT AASHGSLGIF APSSTEEDDG LRNRKVGEQK VQTSL

References

	« Hide 'large scale' referencesShow '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], POSSIBLE FUNCTION. Strain: Paris.
[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
EMBL GenBank DDBJ	CR628336 Genomic DNA. Translation: CAH13280.1.
RefSeq	YP_124440.1. NC_006368.1.
3D structure databases
ProteinModelPortal	Q5X3A8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5X3A8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3119038.
GenomeReviews	Gene locus lpp2128 in contig CR628336_GR.
KEGG	lpp:lpp2128.
PATRIC	22324785. VBILegPne27771_2434.
Organism-specific databases
LegioList	lpp2128.
CMR	Search...
Phylogenomic databases
eggNOG	COG0076.
HOGENOM	HBG657947.
OMA	IIAACWA.
ProtClustDB	CLSK833230.
Enzyme and pathway databases
BioCyc	LPNE297246:LPP2128-MONOMER.
Family and domain databases
InterPro	IPR002129. PyrdxlP-dep_de-COase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KO	K01634.
PANTHER	PTHR11999. Pyridoxal_deC. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SGPL_LEGPA

Accession

Primary (citable) accession number: Q5X3A8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	November 23, 2004
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program