ID   A0A150VGV0_9PEZI        Unreviewed;       579 AA.
AC   A0A150VGV0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=M433DRAFT_58884 {ECO:0000313|EMBL:KYG49563.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG49563.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG49563.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG49563.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG49563.1}.
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DR   EMBL; JPDO01000021; KYG49563.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150VGV0; -.
DR   STRING; 766039.A0A150VGV0; -.
DR   Proteomes; UP000075602; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   MOD_RES         369
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   579 AA;  62931 MW;  66BDFBD2A9533504 CRC64;
     MPGSGRLAVS LPKLNPRKLQ QAGYRQQLLF RTVDFIRNAL LILFILRFTR KTWYHLRGYG
     LLGAFRHAAR DIHRRLYAAF LRLPFVRVKV QQDVDKAIAD LENKLVPSGP GVTHFTALPA
     TGWTVAQIRT ELEKLSEMQH TRWEDGRVSG AVYHGGDELC DLQGEAFRRF GVSNPIHPDV
     FPGVRKMEAE VVAMVLGIFN APPSTINEIG SSMGGGAGVC TSGGTESILM ACLAARNKAR
     AERGVREPEM ILPETAHTAF RKAGEYFGIK IHLVPCPAPT YRLHIPTAAR LINGNTVLLV
     GSAPNFPHGI IDDIPALSRL ALRHKIPLHV DCCLGSFIIP FLVKAGFPSP PDFDFRVPGV
     TSISVDTHKY GFAPKGNSVI LYRNKALRQY QYYICPDWSG GVYASPGLAG SRPGALIAGA
     WASLMRMGED GYLDACLQIV GARQQLEDAV RERPILKASL KVIGKPLVSV LAFRANPNPA
     NAADEVDVYD VADGMSAKGW HLNALQDPPA VHVAVTMPIV RAVNDMIRDL EEVVEAVKGK
     AGTGEKGNAA ALYGVAGSLP DKTIVRELAG GFLDTLYKT
//