ID   SGPL_LEGPH              Reviewed;         601 AA.
AC   Q5ZTI6;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 97.
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=lpg2176;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU28241.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017354; AAU28241.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015444194.1; NC_002942.5.
DR   RefSeq; YP_096188.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZTI6; -.
DR   SMR; Q5ZTI6; -.
DR   STRING; 272624.lpg2176; -.
DR   PaxDb; Q5ZTI6; -.
DR   PRIDE; Q5ZTI6; -.
DR   EnsemblBacteria; AAU28241; AAU28241; lpg2176.
DR   KEGG; lpn:lpg2176; -.
DR   PATRIC; fig|272624.6.peg.2285; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_028929_1_0_6; -.
DR   Proteomes; UP000000609; 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; Reference proteome.
FT   CHAIN           1..601
FT                   /note="Probable sphingosine-1-phosphate lyase"
FT                   /id="PRO_0000248941"
FT   MOD_RES         360
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   601 AA;  66549 MW;  D19C9FF7C61A8A31 CRC64;
     MFGFVSDLLT AAVSSLDELL QDTPAHQIIL GTAALYFLYN QYHNPSISRW YRSRNNASMK
     QRIIDSAYAL AKNLPGVNQI IEKELNKELS STREKLRIQR SGMTLREEIP EEGLSPQDIL
     SAFDVDVEKC HFDFLSVTND SPEREFLVER GDGKDSGALY AIHPKELTEL LKEVYGATAL
     TNPLHDKWPR INAMQAEVIR WCQNLFHGSK ECYGLLTHGG TTSIIEAMAA YVIRARAKGI
     DYPEIVVPET AHAAFKKAAE LTGAILITVP VDKKTGAVNP KVMSSYITRN TAVIVGSAPS
     FMNGIHDPVS ELGQLAKKKN VPFHVDACLG GFLTAFLDTS SEPMDFRVPG VTSISADLHK
     YGCCPKGTSV CLFSEDSPAL SVYAALNWSG GLYATPGILD GSTSGARVAE VYATLSYYGK
     NKYQEIAKSI ITLRNAIQKE LTTLLEEGNG LTSEDIYVYG NPQWSILGFR SNTCNAHFIA
     DELEKRGWKL NLLQNPDGFH LCLTHVHTLV KGFETQFIKD LREAVIDVKN YPPGKKPSGN
     VKVYGAVGMM PIELQREICK QYQKARLNYT SASPGSLRIF TNVPVEEDEG LRNRKTEKYK
     V