SGPL_LEGPA
ID SGPL_LEGPA Reviewed; 605 AA.
AC Q5X3A8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=lpp2128;
OS Legionella pneumophila (strain Paris).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND POSSIBLE FUNCTION.
RC STRAIN=Paris;
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; CR628336; CAH13280.1; -; Genomic_DNA.
DR PDB; 4W8I; X-ray; 2.85 A; A/B=56-605.
DR PDBsum; 4W8I; -.
DR AlphaFoldDB; Q5X3A8; -.
DR SMR; Q5X3A8; -.
DR KEGG; lpp:lpp2128; -.
DR LegioList; lpp2128; -.
DR HOGENOM; CLU_028929_1_0_6; -.
DR OMA; DPHKMGL; -.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Pyridoxal phosphate.
FT CHAIN 1..605
FT /note="Probable sphingosine-1-phosphate lyase"
FT /id="PRO_0000248940"
FT REGION 580..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 360
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 221..238
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:4W8I"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 289..299
FT /evidence="ECO:0007829|PDB:4W8I"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:4W8I"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 351..362
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 380..385
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 406..442
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:4W8I"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:4W8I"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 476..480
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:4W8I"
FT TURN 494..497
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 505..509
FT /evidence="ECO:0007829|PDB:4W8I"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:4W8I"
FT HELIX 513..528
FT /evidence="ECO:0007829|PDB:4W8I"
SQ SEQUENCE 605 AA; 66481 MW; 5EEA8D767A4E38C3 CRC64;
MFGFISDLLT AAVSSLDELL QDTPAHQIIL GTAALYFLYN QYHNPSISRW CRSRNNASMK
QRIIDSAYAL AKNLPGVNQI IEKELNKELS STREKLRIQR SGMTLREEIP EEGLSPQDIL
SAFDVDVEKC HFDFLSVTND SPEREFLVGR GDGKDSGALY AIHPKELTEL LKEVYGATAL
TNPLHDKWPR INAMQAEVIR WCQNLFHGSK EGYGLLTHGG TTSIIEAMAA YVIRARAKGI
DYPEIVVPET AHAAFKKAAE LTGAILITVP VDKKTGAVNP NVMSSYITRN TAVMVGSAPS
FMNGIHDPIS ELGQLAKKKN VPFHVDACLG GFLTAFLDTS SEPMDFRVPG VTSISADLHK
YGCCPKGTSV CLFSEDSPAL SVYAALNWSG GLYATPGILD GSTSGARVAE VYATLSYYGK
NKYQEIAKSI IRLRNAIQKE LTALVEEGNG LTSEDIYVYG NPQWSILGFR SNTCNAHFIA
DELEKRGWKL NLLQNPDGFH LCLTHVHTLV GSFETQFIKD LREAVIDVKN YPPGKKPSGN
VKVYGAVGMM PVELQKEICK QYQKARLDFT AASHGSLGIF APSSTEEDDG LRNRKVGEQK
VQTSL
