LMPD Database

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LMP007212

UniProt Annotations

Entry Information
Gene Nameserine C-palmitoyltransferase LCB1
Protein EntryLCB1_YEAST
UniProt IDP25045
SpeciesYeast (S288c)
Comments
Comment typeDescription
Catalytic ActivityPalmitoyl-CoA + L-serine = CoA + 3-dehydro-D- sphinganine + CO(2). {ECO:0000269|PubMed:10713067, ECO:0000269|PubMed:11781309, ECO:0000269|PubMed:15485854, ECO:0000269|PubMed:8058731}.
CofactorName=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
DomainThe first transmembrane domain is not required for stability, membrane association, interaction with LCB2, or enzymatic activity. The second and third transmembrane domains are required for stability and interaction with LCB2.
FunctionComponent of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine. {ECO:0000269|PubMed:11781309, ECO:0000269|PubMed:8058731}.
InteractionP40970:LCB2; NbExp=9; IntAct=EBI-10059, EBI-10067;
MiscellaneousPresent with 22400 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
PathwayLipid metabolism; sphingolipid metabolism.
SimilarityBelongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
Subcellular LocationCytoplasm. Endoplasmic reticulum membrane; Multi-pass membrane protein.
SubunitLCB1 and LCB2 encode essential subunits of the enzyme and form a heterodimer. Component of the SPOTS complex, at least composed of LCB1/2 (LCB1 and/or LCB2), ORM1/2 (ORM1 and/or ORM2), SAC1 and TSC3. Interacts with LCB2 and TSC3. {ECO:0000269|PubMed:10713067, ECO:0000269|PubMed:11781309, ECO:0000269|PubMed:15485854, ECO:0000269|PubMed:20182505, ECO:0000269|PubMed:8058731}.