ID J8Q0T2_SACAR Unreviewed; 589 AA.
AC J8Q0T2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=SU7_2656 {ECO:0000313|EMBL:EJS42266.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS42266.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS42266.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
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:EJS42266.1}.
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DR EMBL; ALIE01000155; EJS42266.1; -; Genomic_DNA.
DR AlphaFoldDB; J8Q0T2; -.
DR HOGENOM; CLU_028929_1_0_1; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000006968; Chromosome XIII.
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:UP000006968}.
FT MOD_RES 380
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 589 AA; 65566 MW; B201F200AE5EBC22 CRC64;
MGEILNETLS NSDWYGTSVR LLFEDCDFKQ FLILIVSESR RSIYDYFTST PWYSILKDYM
FLTFCYKVIS NLLYLLKVYG PVRLVARTYE HTSRAVFHWL LDSPFLKGTV DKEVSKIKQS
IEDELIKSDS QLMNFPRLPS DGVPQDDVIE ELNKLNDLIP HTQWKEGKVS GAVYHGGDDL
IHLQTVAYEK YCVANQLHPD VFPAVRKMES EVVSMVLRMF NAPIDTGCGT TTSGGTESLL
LACLSAKMYA LHHRGITEPE IIAPTTAHAG FDKAAYYFNM KLRHVELDPK TFQVNLKKVK
KFINKNTVLL VGSAPNFPHG IADDIEGLGQ IAQKYKLPLH VDSCLGSFIV SFMEKAGYKN
LPLLDFRVPG VTSISCDTHK YGFAPKGSSV IMYRNSDLRM HQYYVNPAWT GGLYGSPTLA
GSRPGAIVVG CWATMVNIGE NGYIESCREI VGAAMKFKAF ILESIPDLEI MGNPRYSVVS
FSSKTLNIHE LSDRLAKKGW HFNALQRPVA LHMAFTRLSA HVVDEICDVL RTTVQELKNE
SGSKPSPDGT SALYGVAGSV KTAGVADKLI VGFLDALYKL GPGEDTNVK
//