You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Yeast Metabolome Database.
Identification
NameSerine palmitoyltransferase 1
Synonyms
  • SPT 1
  • SPT1
  • Long chain base biosynthesis protein 1
Gene NameLCB1
Enzyme Class
Biological Properties
General FunctionInvolved in transferase activity, transferring nitrogenous groups
Specific 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
Cellular LocationCytoplasm. Endoplasmic reticulum membrane; Multi-pass membrane protein
SMPDB Pathways
Biosynthesis of unsaturated fatty acidsPW002403 ThumbThumb?image type=greyscaleThumb?image type=simple
Biosynthesis of unsaturated fatty acids (icosanoyl)PW002434 ThumbThumb?image type=greyscaleThumb?image type=simple
Biosynthesis of unsaturated fatty acids (stearoyl)PW002435 ThumbThumb?image type=greyscaleThumb?image type=simple
Sphingolipid metabolismPW002479 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Biosynthesis of unsaturated fatty acidsec01040 Map01040
Sphingolipid metabolismec00600 Map00600
SMPDB Reactions
L-2-amino-3-oxobutanoic acid + Coenzyme AAcetyl-CoA + Glycine
Palmityl-CoA + L-Serine + hydron Coenzyme A + Carbon dioxide + 3-Dehydrosphinganine
Palmityl-CoA + L-Serine3-Dehydrosphinganine + Carbon dioxide
KEGG Reactions
Palmityl-CoA + L-Serine3-Dehydrosphinganine + Carbon dioxide + Coenzyme A
Metabolites
YMDB IDNameView
YMDB00016GlycineShow
YMDB00045Coenzyme AShow
YMDB00112L-SerineShow
YMDB001833-DehydrosphinganineShow
YMDB00301Palmityl-CoAShow
YMDB00312Acetyl-CoAShow
YMDB00527palmitoyl-CoAShow
YMDB00695L-2-amino-3-oxobutanoic acidShow
YMDB00862hydronShow
YMDB00912Carbon dioxideShow
GO Classification
Component
Not Available
Function
cofactor binding
pyridoxal phosphate binding
catalytic activity
transferase activity
binding
transferase activity, transferring nitrogenous groups
Process
metabolic process
biosynthetic process
Gene Properties
Chromosome Locationchromosome 13
LocusYMR296C
Gene Sequence>1677 bp ATGGCACACATCCCAGAGGTTTTACCCAAATCAATACCGATTCCGGCATTTATTGTTACC ACCTCATCGTACCTATGGTACTACTTCAATCTGGTGTTGACTCAAATCCCGGGAGGCCAA TTCATCGTTTCGTACATCAAGAAATCGCATCATGACGATCCATACAGGACCACGGTTGAG ATAGGGCTTATTTTATACGGGATCATCTATTACTTGTCCAAGCCACAACAGAAAAAGAGT CTTCAAGCACAGAAGCCCAACCTATCGCCCCAGGAGATTGACGCGCTAATTGAGGACTGG GAGCCCGAGCCTCTAGTCGACCCTTCTGCCACCGATGAGCAATCGTGGAGGGTGGCCAAA ACACCCGTCACCATGGAAATGCCCATTCAGAACCATATTACTATCACCAGAAACAACCTG CAGGAGAAGTATACCAATGTTTTCAATTTGGCCTCGAACAACTTTTTGCAATTGTCCGCT ACGGAGCCCGTGAAAGAAGTGGTCAAGACCACTATCAAGAATTACGGTGTGGGCGCCTGT GGTCCCGCCGGGTTCTACGGTAACCAGGACGTTCATTACACGTTGGAATATGATTTAGCA CAGTTCTTTGGCACCCAAGGTTCCGTTCTGTACGGGCAAGACTTTTGTGCCGCACCCTCT GTTCTGCCTGCTTTCACAAAGCGTGGTGATGTTATCGTGGCAGACGACCAGGTGTCATTA CCAGTGCAAAATGCTCTGCAACTAAGCAGATCCACAGTCTACTACTTCAACCACAACGAT ATGAATTCGCTAGAATGTTTATTAAACGAGTTGACCGAACAGGAGAAACTTGAGAAACTG CCCGCCATTCCAAGAAAATTTATCGTCACTGAGGGTATTTTCCACAACTCGGGCGATTTA GCTCCGTTGCCTGAGTTGACTAAGCTGAAGAACAAGTACAAGTTCAGACTATTTGTTGAC GAAACCTTCTCCATTGGTGTTCTTGGCGCTACGGGCCGTGGGTTGTCAGAGCACTTCAAC ATGGATCGCGCAACTGCCATTGACATTACCGTTGGGTCCATGGCCACCGCGTTGGGGTCC ACCGGTGGTTTTGTCCTGGGTGACAGTGTTATGTGTTTGCACCAGCGTATTGGTTCCAAT GCATATTGTTTTTCTGCCTGTTTGCCGGCTTACACCGTCACATCCGTCTCCAAAGTCTTG AAATTGATGGACTCCAACAACGACGCCGTCCAGACGCTGCAAAAACTATCCAAATCTTTG CATGATTCCTTTGCATCTGACGACTCCTTGCGTTCATACGTAATCGTCACGTCCTCTCCA GTGTCTGCTGTCCTACATCTGCAACTGACTCCCGCATATAGGTCTCGCAAGTTCGGATAC ACCTGCGAACAGCTATTCGAAACCATGTCAGCTTTGCAAAAGAAGTCCCAGACAAACAAA TTCATTGAGCCATACGAAGAGGAGGAAAAATTTCTGCAGTCCATAGTAGATCATGCTCTT ATTAACTACAACGTTCTCATCACAAGAAACACTATTGTTTTAAAACAGGAGACGCTACCA ATTGTCCCTAGCTTGAAAATCTGCTGTAACGCCGCCATGTCCCCAGAGGAACTCAAAAAT GCTTGCGAAAGTGTCAAGCAGTCCATCCTTGCCTGTTGCCAAGAATCTAATAAATAA
Protein Properties
Pfam Domain Function
Protein Residues558
Protein Molecular Weight62206.60156
Protein Theoretical pI6.1
Signalling Regions
  • None
Transmembrane Regions
  • 50-84
  • 342-371
  • 425-457
Protein Sequence>Serine palmitoyltransferase 1 MAHIPEVLPKSIPIPAFIVTTSSYLWYYFNLVLTQIPGGQFIVSYIKKSHHDDPYRTTVE IGLILYGIIYYLSKPQQKKSLQAQKPNLSPQEIDALIEDWEPEPLVDPSATDEQSWRVAK TPVTMEMPIQNHITITRNNLQEKYTNVFNLASNNFLQLSATEPVKEVVKTTIKNYGVGAC GPAGFYGNQDVHYTLEYDLAQFFGTQGSVLYGQDFCAAPSVLPAFTKRGDVIVADDQVSL PVQNALQLSRSTVYYFNHNDMNSLECLLNELTEQEKLEKLPAIPRKFIVTEGIFHNSGDL APLPELTKLKNKYKFRLFVDETFSIGVLGATGRGLSEHFNMDRATAIDITVGSMATALGS TGGFVLGDSVMCLHQRIGSNAYCFSACLPAYTVTSVSKVLKLMDSNNDAVQTLQKLSKSL HDSFASDDSLRSYVIVTSSPVSAVLHLQLTPAYRSRKFGYTCEQLFETMSALQKKSQTNK FIEPYEEEEKFLQSIVDHALINYNVLITRNTIVLKQETLPIVPSLKICCNAAMSPEELKN ACESVKQSILACCQESNK
References
External Links
ResourceLink
Saccharomyces Genome Database LCB1
Uniprot IDP25045
Uniprot NameLCB1_YEAST
GenBank Gene IDAY693052
Genebank Protein ID51013555
General Reference
  • Buede, R., Rinker-Schaffer, C., Pinto, W. J., Lester, R. L., Dickson, R. C. (1991). "Cloning and characterization of LCB1, a Saccharomyces gene required for biosynthesis of the long-chain base component of sphingolipids." J Bacteriol 173:4325-4332.2066332
  • Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Nagiec, M. M., Baltisberger, J. A., Wells, G. B., Lester, R. L., Dickson, R. C. (1994). "The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis." Proc Natl Acad Sci U S A 91:7899-7902.8058731
  • Gable, K., Slife, H., Bacikova, D., Monaghan, E., Dunn, T. M. (2000). "Tsc3p is an 80-amino acid protein associated with serine palmitoyltransferase and required for optimal enzyme activity." J Biol Chem 275:7597-7603.10713067
  • Gable, K., Han, G., Monaghan, E., Bacikova, D., Natarajan, M., Williams, R., Dunn, T. M. (2002). "Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase." J Biol Chem 277:10194-10200.11781309
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Han, G., Gable, K., Yan, L., Natarajan, M., Krishnamurthy, J., Gupta, S. D., Borovitskaya, A., Harmon, J. M., Dunn, T. M. (2004). "The topology of the Lcb1p subunit of yeast serine palmitoyltransferase." J Biol Chem 279:53707-53716.15485854
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950
  • Breslow, D. K., Collins, S. R., Bodenmiller, B., Aebersold, R., Simons, K., Shevchenko, A., Ejsing, C. S., Weissman, J. S. (2010). "Orm family proteins mediate sphingolipid homeostasis." Nature 463:1048-1053.20182505