3-hydroxyacyl-CoA dehydratase PHS1 (P40857)

Identification
Name3-hydroxyacyl-CoA dehydratase PHS1
Synonyms
  • HACD
  • PTPLA homolog involved in sphingolipid biosynthesis protein 1
Gene NamePHS1
Enzyme Class
Biological Properties
General FunctionInvolved in enoyl-CoA hydratase activity
Specific FunctionResponsible for the dehydration step in very long-chain fatty acids (VLCFAs) synthesis
Cellular LocationEndoplasmic reticulum membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
3-hydroxyacyl-CoA ↔ trans-2,3-didehydroacyl-CoA + water
Metabolites
YMDB IDNameView
YMDB00890waterShow
GO ClassificationNot Available
Gene Properties
Chromosome Locationchromosome 10
LocusYJL097W
Gene Sequence>654 bp ATGTCAAAAAAACTTGCGTCACCATTGTCCTTCTTACCCCTTTATAATTTGCTTTCTGCT GTTGGTTGGTCTTATTTGCTTTACTTGGTCATCTCCTTGTACCCAAAAGTTGGACAGCCA GCATTCTTCTACCAAACTAAAAATGTCGCTACCCTTGTTCAATGTGGTGCTATAATCGAG ATCATAAACTCATTTTTAGGAGTTGTACGTTCCCCATTGCTGACCACTGTTGCACAAGTG TCTTCAAGACTACTAGTTGTCCTCGGCATCTTCCAATTGTTGCCAAACACAAGTGGTGTT CAATCAGTTGTTTACATATCATTATTACTGGCATGGTCTATAACTGAGATCGTCAGATAC TTGTATTATTTTTTCATGTTGGTATTCAAGAATGGCGCACCAAAGATCTTAATTCTATTA AGATATAATTTGTTCTGGATTTTGTACCCCACTGGTGTTGCCAGCGAACTACGCATTATT TACTGTGCTTTAAATGCAGCTGAATCTCAGTATTCTTTACTTTACAAAAGAATTTTAATA GCGGCCATGCTCGCTTATATCCCAGGCTTCCCAATGCTCTTCCTACACATGGTAGCACAG AGAAAGAAAGTCATGAAAAGTTTAAGATCCTCTTTCGGGAAGAAACTAATTTGA
Protein Properties
Pfam Domain Function
Protein Residues217
Protein Molecular Weight24510.40039
Protein Theoretical pI10.37
Signalling Regions
  • None
Transmembrane Regions
  • 12-29
  • 48-66
  • 77-94
  • 100-117
  • 143-160
  • 179-196
Protein Sequence>3-hydroxyacyl-CoA dehydratase PHS1 MSKKLASPLSFLPLYNLLSAVGWSYLLYLVISLYPKVGQPAFFYQTKNVATLVQCGAIIE IINSFLGVVRSPLLTTVAQVSSRLLVVLGIFQLLPNTSGVQSVVYISLLLAWSITEIVRY LYYFFMLVFKNGAPKILILLRYNLFWILYPTGVASELRIIYCALNAAESQYSLLYKRILI AAMLAYIPGFPMLFLHMVAQRKKVMKSLRSSFGKKLI
References
External Links
ResourceLink
Saccharomyces Genome Database PHS1
Uniprot IDP40857
Uniprot NamePHS1_YEAST
GenBank Gene IDAY557855
Genebank Protein ID45269601
General Reference
  • Miosga, T., Boles, E., Schaaff-Gerstenschlager, I., Schmitt, S., Zimmermann, F. K. (1994). "Sequence and function analysis of a 9.74 kb fragment of Saccharomyces cerevisiae chromosome X including the BCK1 gene." Yeast 10:1481-1488.7871887
  • Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
  • 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
  • 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
  • Kim, H., Melen, K., Osterberg, M., von Heijne, G. (2006). "A global topology map of the Saccharomyces cerevisiae membrane proteome." Proc Natl Acad Sci U S A 103:11142-11147.16847258
  • Denic, V., Weissman, J. S. (2007). "A molecular caliper mechanism for determining very long-chain fatty acid length." Cell 130:663-677.17719544
  • Kihara, A., Sakuraba, H., Ikeda, M., Denpoh, A., Igarashi, Y. (2008). "Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation." J Biol Chem 283:11199-11209.18272525