ID W5MNQ3_LEPOC Unreviewed; 473 AA.
AC W5MNQ3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Serine palmitoyltransferase 1 {ECO:0000256|ARBA:ARBA00041066};
DE EC=2.3.1.50 {ECO:0000256|ARBA:ARBA00013220};
DE AltName: Full=Long chain base biosynthesis protein 1 {ECO:0000256|ARBA:ARBA00041765};
DE AltName: Full=Serine-palmitoyl-CoA transferase 1 {ECO:0000256|ARBA:ARBA00042649};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010012.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000010012.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine +
CC CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65073;
CC Evidence={ECO:0000256|ARBA:ARBA00036980};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684;
CC Evidence={ECO:0000256|ARBA:ARBA00036980};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-serine + tetradecanoyl-CoA = 3-oxohexadecasphinganine
CC + CO2 + CoA; Xref=Rhea:RHEA:35675, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:71007;
CC Evidence={ECO:0000256|ARBA:ARBA00035775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676;
CC Evidence={ECO:0000256|ARBA:ARBA00035775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 +
CC CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58299; EC=2.3.1.50;
CC Evidence={ECO:0000256|ARBA:ARBA00036326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC Evidence={ECO:0000256|ARBA:ARBA00036326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + L-serine = 3-oxotetradecasphinganine +
CC CO2 + CoA; Xref=Rhea:RHEA:35679, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:71008;
CC Evidence={ECO:0000256|ARBA:ARBA00036641};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680;
CC Evidence={ECO:0000256|ARBA:ARBA00036641};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHAT01002723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MNQ3; -.
DR STRING; 7918.ENSLOCP00000010012; -.
DR Ensembl; ENSLOCT00000010024.1; ENSLOCP00000010012.1; ENSLOCG00000008246.1.
DR eggNOG; KOG1358; Eukaryota.
DR GeneTree; ENSGT00550000074872; -.
DR HOGENOM; CLU_015846_0_1_1; -.
DR InParanoid; W5MNQ3; -.
DR OMA; GTIDTHE; -.
DR Proteomes; UP000018468; Linkage group LG2.
DR Bgee; ENSLOCG00000008246; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR PANTHER; PTHR13693:SF2; SERINE PALMITOYLTRANSFERASE 1; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..462
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 473 AA; 53365 MW; 2C94D52825B68229 CRC64;
KMASGQQWVL VEMVQAFYEA PAYHLILEGI LILWIIRLLF SKTYKLQDRS DLTDKEKEEL
IEEWQPEPLV PPVSKDHPSL NYDVVSGPPS HNITVNGKEC INFASFNFLG MLENERVKNK
ALASLKKYGV GTCGPRGFYG TFDVHLELEE RLAKFMRTEE AIIYSYGFAT IASAIPAYSK
RGDIVFVDEA ACFSIQKGLQ ASRSFIKYFK HNDMEDLERL LKEQEIEDQK NPRKARVTRR
FIVVEGLYVN TGDICPLPEL VKLKYKYKVR IFLEESLSFG VLGEHGRGVT EHFGVNIDDI
DLISANMENA LASVGGFCCG RSFVIDHQRL SGQGYCFSAS LPPMLAAAAI EALNIMEEDP
EIFTILRNKC KHIHNALQGI SGLKVVGEYF SPAFHLQLKK TTGSRESDVK LLRAIVDYCM
DRQIALTQAH YLDKEEKNLP PPTVRVVVTV QQTEEELEMA AALIKEAAQS ILK
//