ID G1S279_NOMLE Unreviewed; 566 AA.
AC G1S279;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 62.
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 Name=SGPL1 {ECO:0000313|Ensembl:ENSNLEP00000019617.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000019617.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000019617.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000019617.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; ADFV01064349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1S279; -.
DR Ensembl; ENSNLET00000020607.3; ENSNLEP00000019617.2; ENSNLEG00000016177.3.
DR eggNOG; KOG1383; Eukaryota.
DR GeneTree; ENSGT00390000000046; -.
DR HOGENOM; CLU_028929_1_1_1; -.
DR TreeFam; TF300777; -.
DR Proteomes; UP000001073; Chromosome 18.
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 CDD; cd06450; DOPA_deC_like; 1.
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:UP000001073}.
FT MOD_RES 351
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 566 AA; 63283 MW; 0E07E72FFF529ED6 CRC64;
LPSLPLLKAF EPYLEILEVY STKAKNYVNG HCTKYEPWQL IAWSVVWTLL IVWGYEFVFQ
PESLWSRFKK KCFKLTRKMP IIGRKIQDKL NKTKDDISKN MSFLKVDKEY VKALPSQGLS
SSAVLEKLKE YSSMDVFWQE GRASGTVYSG EEKLTELLVK AYGDFAWSNP LHPDIFPGLR
KIEAEIVRIA CSLFNGGPDS CGCVTSGGTE SILMACKAYR DLAFEKGIKT PEIVAPQSAH
AAFNKAASYF GMKIVRVPLT KMMEVDVRAM RRAISRNTAM LVCSTPQFPH GVIDPVPEVA
KLAVKYKIPL HVDACLGGFL IVFMEKAGYP LEHPFDFRVK GVTSISADTH KYGYAPKGSS
LVLYSDKKYR NYQFFVDTDW QGGIYASPTI AGSRPGGISA ACWAALMHFG ENGYVEATKQ
IIKTARFLKS ELENIKGIFV FGNPQLSVIA LGSRDFDIYR LSNLMTAKGW NLNQLQFPPS
IHFCITLLHA RKRVAIQFLK DIRESVTQIM KNPKAKTTGM GAIYGMAQTT VDRNMVAKLS
SVFLDSLYST DTVTQGSQMN GSPKPH
//
