ID   A0A024T870_9STRA        Unreviewed;       601 AA.
AC   A0A024T870;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=sphinganine-1-phosphate aldolase {ECO:0000256|ARBA:ARBA00038965};
DE            EC=4.1.2.27 {ECO:0000256|ARBA:ARBA00038965};
DE   AltName: Full=Sphingosine-1-phosphate aldolase {ECO:0000256|ARBA:ARBA00042568};
GN   ORFNames=H310_14990 {ECO:0000313|EMBL:ETV90178.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV90178.1};
RN   [1] {ECO:0000313|EMBL:ETV90178.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV90178.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC       1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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DR   EMBL; KI914071; ETV90178.1; -; Genomic_DNA.
DR   RefSeq; XP_008881189.1; XM_008882967.1.
DR   AlphaFoldDB; A0A024T870; -.
DR   STRING; 157072.A0A024T870; -.
DR   EnsemblFungi; H310_14990-t26_1; H310_14990-t26_1-p1; H310_14990.
DR   EnsemblProtists; ETV90178; ETV90178; H310_14990.
DR   GeneID; 20092040; -.
DR   VEuPathDB; FungiDB:H310_14990; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   OrthoDB; 3024111at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 6.10.140.2150; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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   PANTHER; PTHR42735; -; 1.
DR   PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        82..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   MOD_RES         405
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   601 AA;  65232 MW;  541C5B2139F8529A CRC64;
     MLAFDAVAVA TAFAAGYVTL GHITHVERLL TKTTPIAVLA FLAYRSYELE QGGAAISRSF
     LVDVLAWGSK HFPLITSLTG DAIVIFGALY LVTSIVPVLR RARYSYSKKK MINVFGQVGI
     SILKRIPILW TRYRNEIRKL EVQIERSLQE HAKSAADFPK QFTLPEKGTS SEVVLSTMKA
     MVKGEDNRWK DGLVSGAVYH GDDDHVGLLN QAYALFNVTN PLHADLWPSV VRMEAEVISM
     TASFLNGGNT EVCGALTSGG TESIVLATKT HRDWFRHDHG ITKPEIIAAV TAHAAIDKAC
     DMLGIRLIKV PVDPVTFRID VAAVKWNISA NTILIYASAP SFPQGTIDDI EALSKVAVTY
     GIGLHVDCCL GGFVLPFAKA LGYPDIPSFD FSLPGVTSMS CDTHKYGYAS KGTSIVLYKS
     KEVRRFQYFA YSDWTGGLYA TPTIAGSRPG ALSAACWASM MRMGREGYLE KTRSIMETVK
     VIKAGIATID GLHLLGAGAA MIVCFGSREL NILKVSDQLT KLGWSLNALQ HPTSVHLCVT
     CRQIGKGDQF VTALREAVEA VKKDPNGKLE GGSAMYGMAS SMPAGPVEDI LRIYQDCTLS
     L
//