ID   A0A395SMG3_FUSSP        Unreviewed;       572 AA.
AC   A0A395SMG3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=FSPOR_1994 {ECO:0000313|EMBL:RGP73618.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP73618.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP73618.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP73618.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP73618.1}.
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DR   EMBL; PXOF01000026; RGP73618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395SMG3; -.
DR   STRING; 5514.A0A395SMG3; -.
DR   Proteomes; UP000266152; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT   MOD_RES         360
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   572 AA;  62677 MW;  AA4AC1F1FDDECAA2 CRC64;
     MASPPHIGSL SRLPANLRGS IESVKRGGHN VSWPLLNLDL LRNVLLFLFF WRWSRRAFWQ
     LRGRGIIGSV VELYTNIRRI LYGYFLRAPG VRGKVQQQVN ESLVKLSDKL VPKDQIRYLT
     LPKEGFSHDV VRSELENLAN MDHTRWEDGF VSGAVYHGEE ELLALQTEAY GKFTVANPIH
     PDVFPGVRKM EAEVVSMVLS MFHAPPGAAG TSTSGGTDSI LMACLAARQK AYAERGVTEP
     EMILPETGHT AFRKAAEYFK IKLHLVACPA PEYQVDVNAV RRLINPNTVM LVGSAPNFPH
     GIIDDISALS KLALRKNLWL HVDCCLGSFL VPFLERAGFE TQLFDFRLKG VSSISCDTHK
     YGFAPKGNST VLYRTAEHRK FQYFVSPDWS GGVYASPGMA GSRPGALIAG CWASLMTMGE
     SGYIDACTKI VGTAKKITEA IQTTPALGGE LEIMGKPLVS VVAFTARNLN VYDIADGMGA
     KGWHLNALQS PPAIHVAVTL PITKVWEKLI ADLEAVVEEE REKERVRLVE GKGTHGKAMG
     DASALYGVAG SLPNKSVVVD LASGFLDLLY KA
//