ID   SGPL_LEGPL              Reviewed;         605 AA.
AC   Q5WUR6;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Probable sphingosine-1-phosphate lyase;
DE            Short=S1PL;
DE            Short=SP-lyase;
DE            Short=SPL;
DE            EC=4.1.2.27;
DE   AltName: Full=Sphingosine-1-phosphate aldolase;
GN   OrderedLocusNames=lpl2102;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND PROBABLE FUNCTION.
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
RN   [2]
RP   POSSIBLE FUNCTION.
RX   PubMed=16406773; DOI=10.1016/j.mib.2005.12.009;
RA   Brueggemann H., Cazalet C., Buchrieser C.;
RT   "Adaptation of Legionella pneumophila to the host environment: role of
RT   protein secretion, effectors and eukaryotic-like proteins.";
RL   Curr. Opin. Microbiol. 9:86-94(2006).
CC   -!- FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as
CC       sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine
CC       (By similarity). Possibly implicated in influencing the macrophage
CC       autophagy pathway. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sphinganine 1-phosphate = hexadecanal + phosphoethanolamine;
CC         Xref=Rhea:RHEA:18593, ChEBI:CHEBI:17600, ChEBI:CHEBI:57939,
CC         ChEBI:CHEBI:58190; EC=4.1.2.27;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC       1-phosphate lyase subfamily. {ECO:0000305}.
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DR   EMBL; CR628337; CAH16342.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5WUR6; -.
DR   SMR; Q5WUR6; -.
DR   EnsemblBacteria; CAH16342; CAH16342; lpl2102.
DR   KEGG; lpf:lpl2102; -.
DR   LegioList; lpl2102; -.
DR   HOGENOM; CLU_028929_1_0_6; -.
DR   OMA; FKDHQFT; -.
DR   Proteomes; UP000002517; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..605
FT                   /note="Probable sphingosine-1-phosphate lyase"
FT                   /id="PRO_0000248942"
FT   MOD_RES         360
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   605 AA;  66495 MW;  9D75A08557921015 CRC64;
     MFGFISDLLT AAVSSLDELL QDTPAHQIIL GTAALYFLYN QYHNPSISRW YLSRNNASMK
     QRIIDSAYAL AKNLPGVNQI IEKELNKELS STREKLRIQR SGMTLREEIP EEGLSPQDIL
     SAFDVDVEKC HFDFLSVNND SPEREFLVGG GDGKDSGALY AIHPKELTEL LKEVYGATAL
     TNPLHDKWPR INAMQAEVIR WCQNLFHGSK EGYGLLTHGG TTSIIEAMAA YVIRARAKGI
     DYPEIVVPET AHAAFKKAAE LTGAILITVP VDKKTGAVNP RVMSSYITRN TAVIVGSAPS
     FMNGIHDPVS ELGQLAKKKN VPFHVDACLG GFLTAFLDTS SEPMDFRVPG VTSISADLHK
     YGCCPKGTSV CLFSEDSPAL SVYAALNWSG GLYATPGILD GSTSGARVAE VYATLSYYGK
     NKYQEIAKSI IKLRNAIQKE LTALVEEGNG LTSEDIYVYG NPQWSILGFR SNTCNAHFIA
     DELEKRGWKL NLLQNPDGFH LCLTHVHTLV RGFETQFIKD LREAVIDVKN YPPGKKASGN
     VKVYGAVGMM PIELQKEICK QYQKARLDFT AASHGSLGIF TTSPTEEDDG LRNRKVGEQK
     VQTSL