ID   A0A0A2VRC3_BEABA        Unreviewed;       566 AA.
AC   A0A0A2VRC3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=BBAD15_g6000 {ECO:0000313|EMBL:KGQ08670.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ08670.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ08670.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ08670.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-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:KGQ08670.1}.
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DR   EMBL; ANFO01000558; KGQ08670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2VRC3; -.
DR   STRING; 1245745.A0A0A2VRC3; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_028929_1_0_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IEA:EnsemblFungi.
DR   GO; GO:0019722; P:calcium-mediated signaling; IEA:EnsemblFungi.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblFungi.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:EnsemblFungi.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT   MOD_RES         354
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   566 AA;  61275 MW;  F3F91C2E55CF726B CRC64;
     MPGSSRMPIS LRGSGALKPG TPSALSLGLV NLDLVRNIIF VYFVSRWTRR LYWKLRGRGV
     IGAILELYRD IRRVLYGWFL QAPGVRTQVR AKVKESLDKM AAKLVPPAQT RYLTLPKEGL
     PEETIRAELD SLANMDHTRW EDGYVSGAVY HGEADLIKLQ TDAYGLFTVS NPIHPDVFPG
     VRKMEAEVVS MVLNMFHAPQ GAAGASTSGG TESILLACLA ARQKAYVERG VTEPEMILPI
     TAHTAFRKAG DYFKIKVHFV ECPAPNYQVN LAGVSRLINR NTIMLVGSAP NFPHGIIDDI
     AGLSRLAVRN KLWLHVDCCL GSFVIACLEK AGFEAEPFDF RVKGVSSISV DTHKYGFAPK
     GNSTVLYRTA ALRTYQYYVC PDWAGGVYAS PGLAGSRPGA LIAGCWASLM SVGEAGYVDS
     CAKIVGAAKK IADAIRESPA LAGELEIIGR PLVSVVAFTA QNLDIYDIAD AMSSKGWHLN
     ALQNPPAIHV AVTLPITKVW SKLISDLETA VEEEREKERV RVVEGKGAKG KAVGDSAALY
     GVAGSLPNKS VVVDLATGFL DLLYKA
//