3-ketoacyl-CoA thiolase, peroxisomal (P27796)

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
Fatty acid metabolismPW002460 ThumbThumb?image type=greyscaleThumb?image type=simple
Steroid biosynthesisPW002482 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Biosynthesis of unsaturated fatty acidsec01040 Map01040
Fatty acid elongation in mitochondriaec00062 Map00062
Fatty acid metabolismec00071 Map00071
Steroid biosynthesisec00100 Map00100
Valine, leucine and isoleucine degradationec00280 Map00280
SMPDB Reactions
octanoyl-CoA + Acetyl-CoA ↔ 3-oxodecanoyl-CoA + Coenzyme A
(S)-Hydroxyoctanoyl-CoA + NAD ↔ 3-Oxooctanoyl-CoA + hydron + NADH
Acetyl-CoA + Hexanoyl-CoA ↔ 3-Oxooctanoyl-CoA + Coenzyme A
Acetyl-CoA + Hexanoyl-CoA ↔ 3-Oxooctanoyl-CoA + Coenzyme A
Acetyl-CoA + Hexanoyl-CoA ↔ 3-Oxooctanoyl-CoA + Coenzyme A
KEGG Reactions
3-oxolauroyl-CoA + Coenzyme A → Acetyl-CoA + decanoyl-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
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
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