ID A0A074XDS6_AURPU Unreviewed; 559 AA.
AC A0A074XDS6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=M438DRAFT_327028 {ECO:0000313|EMBL:KEQ80177.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ80177.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ80177.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ80177.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL585000; KEQ80177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XDS6; -.
DR STRING; 1043002.A0A074XDS6; -.
DR HOGENOM; CLU_028929_1_0_1; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000030706; 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:UP000030706}.
FT MOD_RES 349
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 559 AA; 60659 MW; AE8E43FA62C3579E CRC64;
MAPGITTVLD VRTPAARRQL AKTTVDLFRN LLFLLFIVRY SRVALTHLYG YGPIASAKMG
YAALRKSLYR IFLSLPGVRG KVQAEIKQTL EELEKKLVPS GPGITRYTAL PASGWGPEQV
RAELEKLHEM KHTRWEDGRV SGAVYHGGKE LQDLQMEAFG RFGVANPIHP DVFPGVRKME
AEVVAMVLGM FNAPADAAGV STSGGSESII MAVLSAREKA RIERRVTKPE IILPETAHTA
FRKAAAYFKI TVHYVPCPGP TYKASLSHVS RLINSNTILL VGSAPNFPHG IIDDIPGLSR
LALRRNIPLH VDCCLGSFLV PFLERAGYDT EPFDFRVKGV TSISCDTHKY GFAPKGNSTL
LYRSAALRKY QYFISPDWSG GVYASPGIAG SRPGALIAGC WASMMSVGEA GYITSCHQIV
GAAKKMAEGL RSRDTLRNDL RILGKPLVSV VAFTSDTLDI YNIADAMSGK GWHLNALQSP
AAIHVAVTLP IVPVVDELLN DLEACVEEER EKQRQAVVEG KPKAKKGDAA ALYGVAGALP
DKTIVEDLAA GFLDCLYKA
//
