ID   A0A1E3QU09_9ASCO        Unreviewed;       582 AA.
AC   A0A1E3QU09;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=BABINDRAFT_160571 {ECO:0000313|EMBL:ODQ81178.1};
OS   Babjeviella inositovora NRRL Y-12698.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX   NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ81178.1, ECO:0000313|Proteomes:UP000094336};
RN   [1] {ECO:0000313|Proteomes:UP000094336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-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; KV454428; ODQ81178.1; -; Genomic_DNA.
DR   RefSeq; XP_018986506.1; XM_019128316.1.
DR   AlphaFoldDB; A0A1E3QU09; -.
DR   STRING; 984486.A0A1E3QU09; -.
DR   GeneID; 30146169; -.
DR   OrthoDB; 3024111at2759; -.
DR   Proteomes; UP000094336; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094336};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   MOD_RES         367
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   582 AA;  63197 MW;  92AA5F9842AB5E8D CRC64;
     MLDSIISRLK ALDIALQLGV FEEDAVHYYH EMRHQLRYVL LKEVIFLYVV YRIVLYVVLP
     LVQQVYAYGP VTVLQRARKT WTGAFFRWFL ASPLARARVD KEVAKNIANL EGSLIVSAPG
     LCSHSKLPAV GIPTETVLDT LTELSQLKHS AWEAGKVSGA VYHGGDDIIA LQSQAFQKNC
     VANQLHPDVF PGVRKMESEV VAMVLDMYNA PVRACGTSSS GGTESLLLAC LAAKVYGARY
     KGISSPEIVA PVTIHAGVDK AAYYFGIKLH KARVDPKTMQ VDLSQVKRLI NRNTVLLCGS
     SPNFPHGIID DIQGMSDLAV RYDIPLHVDS CLGSFITPFA NKAGFHDVPI CDFRVPGVTS
     ISCDTHKYGF APKGSSVIMY RDNKMRECQY YVNVEWSGGV YGSPTLAGSR PGALMAGCWA
     TMMNIGEDGY VKSAQEIIQA SRDFKAAVQR IPQLRVLGDP LGSVVSFTVA ELASLNIYEL
     SDAMSAKGWH LSTLQTPAAV HIAFTRLSSP VIHELVADLQ SVVDALVEEG IGGKTKPLGD
     TAALYGVAGS VTTTGVIDRL VVGFLDTLYK CDVCTDGSSR EL
//