ID   A0A1S7UKG2_ROSNE        Unreviewed;       569 AA.
AC   A0A1S7UKG2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMD00023353_0501810 {ECO:0000313|EMBL:GAP83775.1};
OS   Rosellinia necatrix (White root-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX   NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP83775.1};
RN   [1] {ECO:0000313|EMBL:GAP83775.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W97 {ECO:0000313|EMBL:GAP83775.1};
RA   Kanematsu S.;
RT   "Draft genome sequence of Rosellinia necatrix.";
RL   Submitted (MAR-2016) 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; DF977450; GAP83775.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S7UKG2; -.
DR   STRING; 77044.A0A1S7UKG2; -.
DR   OMA; AFWQLRG; -.
DR   OrthoDB; 3024111at2759; -.
DR   Proteomes; UP000054516; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IEA:UniProtKB-EC.
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:UP000054516}.
FT   MOD_RES         357
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   569 AA;  62624 MW;  8D498C60BA1451D2 CRC64;
     MPGTSRMPIS LRESLNSVKR ARPVNTVQSL QFINLDLFRN VVFFFFVLRI IRRSFWKLKG
     RGLIGTIVEL YTDARRILYG YFLRAPGIRT QVRKQINESL AKIQAKMIPA DGSRYLTLPK
     EGWTDEALQK ELETLANMDH TRWEDGFVSG AVYHGEDDLL KLQTEAYGKF TVANPIHPDV
     FPGVRKMEAE VVAMVLSMFH APPTAAGVST SGGTESILMA CYSARQKAYA ERGVTEPEMI
     LPETAHTAFR KAGDYFKIKI HLVPCPAPTY QVDVRRVSRL INSNTILLVG SAPNFPHGIM
     DDISALSKLA LKRRLPLHVD CCLGSFLVPF LERAGFETEL FDFRLKGVTS ISCDTHKYGF
     APKGNSTVLY RTQELRTYQY FVSPDWSGGV YASPGIAGSR PGALIAGCWT SMMKVGETGY
     VDACVKIVGC AKKIAEHVAQ SPALAAELDL IGRPLVSVVA FTARNLNIYD IADGMSSKGW
     HLNALQNPPA MHVAVTMPIT KVWERLVADL EAVVEAEREK ERARAVEGKG PKGKATGDTA
     ALYGVAGSLP NKAVVVDLAT GFIDLMYKA
//