ID   A0A0A8L4T1_9SACH        Unreviewed;       582 AA.
AC   A0A0A8L4T1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=KLDO_g1493 {ECO:0000313|EMBL:CDO93191.1};
OS   Kluyveromyces dobzhanskii CBS 2104.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO93191.1, ECO:0000313|Proteomes:UP000031516};
RN   [1] {ECO:0000313|EMBL:CDO93191.1, ECO:0000313|Proteomes:UP000031516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA   Nystedt B., Astrom S.;
RT   "The genome of Kluyveromyces dobzhanskii.";
RL   Submitted (MAR-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDO93191.1}.
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DR   EMBL; CCBQ010000019; CDO93191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8L4T1; -.
DR   OrthoDB; 3024111at2759; -.
DR   Proteomes; UP000031516; Unassembled WGS sequence.
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   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         376
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   582 AA;  64170 MW;  31C5568966F53526 CRC64;
     MTKFGIIEGL QKQFYLGYSY KYNALEFNPA IILTSVKDTV LDYFFSTPWY WIVRDYVFFH
     LVFKVLSQAL TYVRGYGLLR SITELLRYAS KRIFGIVLNL PFLKVAVDKE VSKALSGMEN
     DVIKNDDNLI DFAELPSSGL PKTDVLEELD KLNSILHHSD WKGGKVSGAV YHGGDDLIDL
     QSKAFQKFCV ANQLHPDVFP GVRKMEAEVV SMVLNAFNAP STGCGTTTSG GTESLLLACL
     SAKMLGLHYK GITEPEMIIP RTAHAGFDKA GYYFGIKVHH VDLISETYQA NVKQMKRLIN
     RNTILLVGSA PNFPHGIIDD IASIGRLGET HKIPVHVDCC LGSFIVAFMS KAGFDDVPLF
     DFRVPGVTSI SCDTHKYGFA PKGSSVIMYR NTKLRKEQYY VSTEWVGGLY GSPTLAGSRP
     GALVVGCWAT MIHVGEDGYI KSCKEIVGKA REIKEYIQTE IPELQILGNP LCSVVSFTSN
     IINIYELSDT LAKSGWHLSA LQNPSAVHLA FTKLSLQSAE EFKHLLKSTV DTMKSQPDAK
     PSSDGTSALY GVAGSVKTSG VADRLIEGFL DTLYKLEPDH SD
//