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Identification
Name3-ketoacyl-CoA thiolase, peroxisomal
Synonyms
  • Acetyl-CoA acyltransferase
  • Beta-ketothiolase
  • Peroxisomal 3-oxoacyl-CoA thiolase
Gene NamePOT1
Enzyme Class
Biological Properties
General FunctionInvolved in transferase activity, transferring acyl groups other than amino-acyl groups
Specific FunctionAcyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Cellular LocationPeroxisome
SMPDB Pathways
Biosynthesis of unsaturated fatty acidsPW002403 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(12:0)PW002548 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(16:0)PW002550 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(18:0)PW002551 ThumbThumb?image type=greyscaleThumb?image type=simple
Fatty acid elongation in mitochondriaPW002467 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
alpha-Linolenic acid metabolismec00592 Map00592
SMPDB Reactions
(S)-3-hydroxypalmitoyl-CoAhexadec-2-enoyl-CoA + water
(S)-3-hydroxytetradecanoyl-CoA(2E)-Tetradecenoyl-CoA + water
(S)-3-hydroxydecanoyl-CoA(2E)-Decenoyl-CoA + water
(S)-Hydroxyoctanoyl-CoA(2E)-Octenoyl-CoA + water
(S)-3-hydroxylauroyl-CoA(2E)-Dodecenoyl-CoA + water
KEGG Reactions
3-oxooctadecanoyl-CoA + Coenzyme APalmityl-CoA + Acetyl-CoA
Coenzyme A + 3-oxohexacosanoyl-CoAAcetyl-CoA + Tetracosanoyl-CoA
Coenzyme A + 3-oxopalmitoyl-CoAAcetyl-CoA + Tetradecanoyl-CoA
3-oxotetradecanoyl-CoA + Coenzyme AAcetyl-CoA + lauroyl-CoA
3-oxodecanoyl-CoA + Coenzyme AAcetyl-CoA + octanoyl-CoA
Metabolites
YMDB IDNameView
YMDB00045Coenzyme AShow
YMDB00099Tetradecanoyl-CoA Show
YMDB00110NADShow
YMDB00143NADHShow
YMDB00215(2E)-Dodecenoyl-CoAShow
YMDB00312Acetyl-CoAShow
YMDB00464(S)-3-hydroxydecanoyl-CoAShow
YMDB00465(S)-3-hydroxylauroyl-CoAShow
YMDB00468(S)-3-hydroxypalmitoyl-CoAShow
YMDB00469hexadec-2-enoyl-CoAShow
YMDB00473(S)-3-hydroxytetradecanoyl-CoAShow
YMDB004743-oxodecanoyl-CoAShow
YMDB004753-oxolauroyl-CoAShow
YMDB004763-oxopalmitoyl-CoAShow
YMDB004773-oxooctadecanoyl-CoAShow
YMDB004783-oxotetradecanoyl-CoAShow
YMDB00527palmitoyl-CoAShow
YMDB00528myristoyl-CoAShow
YMDB00529acetoacetyl-CoAShow
YMDB00530lauroyl-CoAShow
YMDB00531octanoyl-CoAShow
YMDB00532decanoyl-CoAShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB00909Tetracosanoyl-CoA Show
YMDB009603-oxohexacosanoyl-CoAShow
YMDB16130Butyryl-CoAShow
YMDB161333-Hydroxybutyryl-CoAShow
YMDB16153Hexanoyl-CoAShow
YMDB16167(S)-Hydroxyoctanoyl-CoAShow
YMDB161683-Oxooctanoyl-CoAShow
YMDB16169(S)-Hydroxyhexanoyl-CoAShow
YMDB161703-Oxohexanoyl-CoAShow
YMDB16172(2E)-Tetradecenoyl-CoAShow
YMDB16173(2E)-Decenoyl-CoAShow
YMDB16174(2E)-Octenoyl-CoAShow
YMDB161853-Oxohexadecanoyl-CoAShow
GO Classification
Component
Not Available
Function
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
catalytic activity
Process
metabolic process
Gene Properties
Chromosome Locationchromosome 9
LocusYIL160C
Gene Sequence>1254 bp ATGTCTCAAAGACTACAAAGTATCAAGGATCATTTGGTGGAGAGCGCCATGGGTAAGGGT GAATCGAAGAGGAAGAACTCGTTGCTGGAGAAAAGACCCGAAGATGTAGTTATTGTGGCT GCTAACAGGTCTGCCATCGGTAAAGGTTTTAAAGGTGCCTTCAAAGATGTAAACACAGAC TACTTATTATACAACTTTCTCAATGAGTTCATCGGGAGGTTTCCGGAACCTTTGAGGGCT GATTTGAACTTAATCGAAGAAGTTGCCTGTGGAAATGTTCTCAATGTTGGAGCCGGTGCT ACAGAACACAGGGCTGCATGCTTGGCAAGTGGGATTCCCTACTCGACGCCATTTGTCGCT TTAAACAGACAATGTTCTTCAGGTTTAACGGCGGTGAACGATATTGCCAACAAGATTAAG GTTGGGCAAATTGATATTGGTTTGGCGCTGGGAGTGGAATCAATGACCAATAACTACAAA AACGTCAATCCCTTGGGCATGATCTCCTCTGAAGAGCTGCAAAAAAACCGAGAAGCGAAG AAATGTCTAATACCAATGGGCATTACTAATGAGAATGTTGCCGCTAATTTCAAGATCAGT AGAAAGGATCAAGACGAGTTCGCTGCGAATTCATATCAAAAAGCTTACAAGGCGAAAAAT GAGGGGCTTTTCGAAGATGAAATTTTACCTATAAAATTACCAGATGGCTCAATTTGCCAG TCGGACGAAGGGCCACGCCCTAACGTCACTGCGGAGTCGCTTTCAAGCATCAGGCCTGCC TTTATCAAAGACAGAGGAACCACAACTGCGGGCAATGCATCCCAGGTCTCCGATGGTGTG GCAGGTGTCTTGTTAGCCCGCAGGTCCGTAGCCAACCAGTTAAATCTGCCTGTGCTAGGT CGCTACATCGATTTTCAAACAGTGGGGGTTCCCCCTGAAATCATGGGTGTGGGCCCTGCA TACGCCATACCAAAAGTCCTGGAAGCTACTGGCTTGCAAGTCCAAGATATCGATATTTTT GAAATAAATGAAGCATTCGCGGCCCAAGCATTATACTGCATCCATAAACTGGGCATCGAT TTGAATAAAGTAAATCCAAGAGGTGGTGCAATCGCGTTAGGCCATCCCTTGGGTTGTACT GGCGCAAGGCAAGTAGCTACCATACTAAGAGAACTGAAAAAGGATCAAATCGGGGTTGTT AGTATGTGTATCGGTACTGGTATGGGTGCCGCCGCCATCTTTATTAAAGAATAG
Protein Properties
Pfam Domain Function
Protein Residues417
Protein Molecular Weight44729.89844
Protein Theoretical pI7.7
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>3-ketoacyl-CoA thiolase, peroxisomal MSQRLQSIKDHLVESAMGKGESKRKNSLLEKRPEDVVIVAANRSAIGKGFKGAFKDVNTD YLLYNFLNEFIGRFPEPLRADLNLIEEVACGNVLNVGAGATEHRAACLASGIPYSTPFVA LNRQCSSGLTAVNDIANKIKVGQIDIGLALGVESMTNNYKNVNPLGMISSEELQKNREAK KCLIPMGITNENVAANFKISRKDQDEFAANSYQKAYKAKNEGLFEDEILPIKLPDGSICQ SDEGPRPNVTAESLSSIRPAFIKDRGTTTAGNASQVSDGVAGVLLARRSVANQLNLPVLG RYIDFQTVGVPPEIMGVGPAYAIPKVLEATGLQVQDIDIFEINEAFAAQALYCIHKLGID LNKVNPRGGAIALGHPLGCTGARQVATILRELKKDQIGVVSMCIGTGMGAAAIFIKE
References
External Links
ResourceLink
Saccharomyces Genome Database POT1
Uniprot IDP27796
Uniprot NameTHIK_YEAST
GenBank Gene IDAY693184
Genebank Protein ID51013819
PDB ID
1AFW
General Reference
  • Einerhand, A. W., Voorn-Brouwer, T. M., Erdmann, R., Kunau, W. H., Tabak, H. F. (1991). "Regulation of transcription of the gene coding for peroxisomal 3-oxoacyl-CoA thiolase of Saccharomyces cerevisiae." Eur J Biochem 200:113-122.1715273
  • Igual, J. C., Matallana, E., Gonzalez-Bosch, C., Franco, L., Perez-Ortin, J. E. (1991). "A new glucose-repressible gene identified from the analysis of chromatin structure in deletion mutants of yeast SUC2 locus." Yeast 7:379-389.1872029
  • Churcher, C., Bowman, S., Badcock, K., Bankier, A., Brown, D., Chillingworth, T., Connor, R., Devlin, K., Gentles, S., Hamlin, N., Harris, D., Horsnell, T., Hunt, S., Jagels, K., Jones, M., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Rowley, N., Skelton, J., Smith, V., Barrell, B., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Nature 387:84-87.9169870
  • 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
  • Glover, J. R., Andrews, D. W., Subramani, S., Rachubinski, R. A. (1994). "Mutagenesis of the amino targeting signal of Saccharomyces cerevisiae 3-ketoacyl-CoA thiolase reveals conserved amino acids required for import into peroxisomes in vivo." J Biol Chem 269:7558-7563.8125978
  • Mathieu, M., Zeelen, J. P., Pauptit, R. A., Erdmann, R., Kunau, W. H., Wierenga, R. K. (1994). "The 2.8 A crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered alpha beta alpha beta alpha structure constructed from two core domains of identical topology." Structure 2:797-808.7812714
  • Mathieu, M., Modis, Y., Zeelen, J. P., Engel, C. K., Abagyan, R. A., Ahlberg, A., Rasmussen, B., Lamzin, V. S., Kunau, W. H., Wierenga, R. K. (1997). "The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism." J Mol Biol 273:714-728.9402066