ID   A0A024GNG5_9STRA        Unreviewed;       610 AA.
AC   A0A024GNG5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=BN9_094870 {ECO:0000313|EMBL:CCI48403.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI48403.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI48403.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI48403.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) 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:CCI48403.1}.
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DR   EMBL; CAIX01000221; CCI48403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GNG5; -.
DR   STRING; 65357.A0A024GNG5; -.
DR   InParanoid; A0A024GNG5; -.
DR   OrthoDB; 3024111at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        54..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   MOD_RES         414
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   610 AA;  67346 MW;  6A432D4742DE5E1D CRC64;
     MFAETHTECP FSELKALEPY IGGTIVTLIL LYIGARCVSL PFNVERILHK SHDTILLAVA
     IYSFYFVKGQ SLLSHFWQLL IKESPDAEKI IGNVIVVLLI FRTLGQSLDV VRKVRYVSYK
     QLLNTFGGAL IDTGKNVPWI ASKMEKRMKS IEVDIQKALK KSQDGQELTE YVELPAQGMP
     DDALIKELKM YAGNADEKWK KGLVSGAVYH GGDEHLAVLN KAFELFSVAN PLHPDLWPSV
     CRMEAQVIAM TTKLFSGGNA DVCGCFSSGG TESILLAAKT HREWYYHKHS IIKPEIIAAQ
     TAHAAIDKAC SILKIKLIKV PVNPVTMKMD CNAVKWNITA NTIMIYASAP NFPSGIIDDV
     EKLSRIAKDN DIGLHVDCCL GGFILPFIKR IRPNLPKYDF VLPGVTSMSC DAHKYGYAAK
     GTSLVLYRNK AIRNYQYFTF PDWTGGLYVT PTIAGSRSGA LSATAWTSLI RLGEAGFIKN
     AEGIVKTAEE IKEGIKKIDG LHVLGDPQLM VVAFASHEFN ILKVNDEMTK RGWSLNALQH
     PHSLHICVTM CHLRAAKNFL RDLEEAVITV KKDPDGAIKG GSAIYGMASS MPAGPVDDIL
     RIYTNLTLEV
//