ID   A0A3B0J331_DROGU        Unreviewed;       545 AA.
AC   A0A3B0J331;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=DGUA_6G001102 {ECO:0000313|EMBL:SPP73603.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP73603.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) 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; OUUW01000001; SPP73603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0J331; -.
DR   STRING; 7266.A0A3B0J331; -.
DR   OMA; DPHKMGL; -.
DR   OrthoDB; 3024111at2759; -.
DR   Proteomes; UP000268350; 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   CDD; cd06450; DOPA_deC_like; 1.
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         342
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   545 AA;  60289 MW;  DB4D781B94936E48 CRC64;
     MRPFSGSDCL KPVTEGINRA FGAREPWQVA TITATTVLGG VWLWTFVCQD ESLYTRGKRQ
     FFRFAKKIPA VRRQVEVELT KANNDFETAI KTSNAHLTYT VTLPEKGLSK EVILKLVDDH
     LKTGHYEWRD GRVSGAVYGY NPELVQLVTE VYGKASYTNP LHADLFPGVC KMEAEVVRMA
     CNLFHGSNDS CGTMTTGGTE SIVMAMKAYR DYAREHKGIT RPNIVVPRTV HAAFDKGGQY
     FNIHVRSVDV DPQTFEVDMK KFKRAINRNT ILLVGSAPNF PYGTIDDIEA IAELGVKYDI
     PVHVDACLGS FVVALVRNAG YKLRPFDFEV KGVTSISADT HKYGFAPKGS SVILYSQKKF
     KDHQFTVTTD WPGGVYGSPT VNGSRAGGII AACWATMMSF GYDGYLEATK RIVDTARYIE
     RGVRDIDGLF VFGKPATSVI ALGSNVFDIF RLSDSLCKLG WNLNALQFPS GIHICVTDMH
     TQAGVADKFI ADVRSCTAEI MKDPGQPVVG KMALYGMAQS IPDRSVIGEV TRLFLHSMYY
     TPSQK
//