Long-chain-fatty-acid--CoA ligase 3 (P39002)

Identification
NameLong-chain-fatty-acid--CoA ligase 3
Synonyms
  • Fatty acid activator 3
  • Long-chain acyl-CoA synthetase 3
Gene NameFAA3
Enzyme Class
Biological Properties
General FunctionInvolved in catalytic activity
Specific FunctionEsterification, concomitant with transport, of endogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. This enzyme acts preferentially on C16 and C18 fatty acids with a cis-double bond at C-9-C-10
Cellular LocationNot Available
SMPDB Pathways
Biosynthesis of unsaturated fatty acidsPW002403 ThumbThumb?image type=greyscaleThumb?image type=simple
Biosynthesis of unsaturated fatty acids (docosanoyl)PW002408 ThumbThumb?image type=greyscaleThumb?image type=simple
Biosynthesis of unsaturated fatty acids (tetracosanoyl-CoA)PW002404 ThumbThumb?image type=greyscaleThumb?image type=simple
Fatty acid metabolismPW002460 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Biosynthesis of unsaturated fatty acidsec01040 Map01040
Fatty acid metabolismec00071 Map00071
SMPDB Reactions
Palmitic acid + Adenosine triphosphate + Coenzyme A → Adenosine monophosphate + Pyrophosphate + Palmityl-CoA
KEGG Reactions
Adenosine triphosphate + Coenzyme A + Palmitic acid ↔ Adenosine monophosphate + Pyrophosphate + Palmityl-CoA
Adenosine triphosphate + Coenzyme A + palmitoleic acid ↔ Adenosine monophosphate + Pyrophosphate + hexadec-2-enoyl-CoA
stearic acid + Adenosine triphosphate + Coenzyme A ↔ Adenosine monophosphate + Pyrophosphate + stearoyl-CoA
Adenosine triphosphate + Coenzyme A + Oleic acid ↔ Adenosine monophosphate + Pyrophosphate + oleoyl-CoA
Adenosine triphosphate + Linoleic acid + Coenzyme A ↔ Adenosine monophosphate + Pyrophosphate
Metabolites
YMDB IDNameView
YMDB00045Coenzyme AShow
YMDB00069Palmitic acidShow
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB001134-Phospho-L-aspartic acidShow
YMDB00219PyrophosphateShow
YMDB00301Palmityl-CoAShow
YMDB00469hexadec-2-enoyl-CoAShow
YMDB00527palmitoyl-CoAShow
YMDB00528myristoyl-CoAShow
YMDB00538stearoyl-CoAShow
YMDB00539oleoyl-CoAShow
YMDB00679myristic acidShow
YMDB00680Myristoleic acidShow
YMDB00681palmitoleic acidShow
YMDB00682stearic acidShow
YMDB00884Linoleic acidShow
GO Classification
Component
Not Available
Function
catalytic activity
Process
metabolic process
Gene Properties
Chromosome Locationchromosome 9
LocusYIL009W
Gene Sequence>2085 bp ATGTCCGAACAACACTCTGTCGCAGTCGGTAAAGCTGCTAATGAGCACGAGACTGCCCCT AGGAGAAATGTTAGAGTCAAGAAGCGGCCCTTAATTAGACCATTGAACTCGTCAGCATCT ACGCTGTATGAATTTGCCCTAGAGTGTTTCAACAAGGGTGGAAAACGAGATGGTATGGCT TGGAGAGATGTCATCGAGATTCATGAGACAAAGAAAACCATTGTGAGAAAGGTAGACGGC AAGGATAAATCTATAGAAAAGACATGGCTGTATTATGAAATGTCACCATATAAAATGATG ACCTACCAGGAACTGATCTGGGTGATGCACGATATGGGCCGTGGGCTGGCAAAAATAGGC ATCAAGCCCAATGGAGAACACAAATTCCACATCTTCGCATCTACTTCCCATAAATGGATG AAGATTTTCCTTGGTTGCATATCCCAGGGTATCCCCGTAGTAACCGCGTATGATACTTTG GGTGAGAGCGGTTTGATTCACTCCATGGTTGAAACCGAGTCTGCTGCTATTTTCACTGAT AATCAATTATTGGCTAAAATGATAGTGCCTTTGCAATCTGCTAAAGATATCAAATTTCTT ATCCATAACGAACCTATCGACCCCAATGACAGAAGACAAAACGGCAAACTTTACAAGGCT GCTAAGGATGCCATTAATAAGATCAGAGAAGTTAGGCCAGACATAAAAATTTATAGTTTT GAAGAAGTTGTCAAGATAGGTAAAAAAAGTAAAGATGAGGTCAAACTTCATCCACCTGAG CCAAAAGATTTGGCTTGTATCATGTACACCTCGGGCTCGATCAGTGCACCAAAAGGTGTA GTATTGACTCATTATAATATTGTTTCGGGTATCGCTGGTGTAGGTCACAACGTCTTTGGA TGGATCGGCTCTACAGACCGTGTTTTGTCGTTCTTGCCATTGGCTCATATTTTTGAACTG GTCTTTGAATTCGAAGCCTTTTACTGGAACGGTATTCTTGGGTACGGTAGTGTTAAGACT TTGACTAATACTTCGACTCGTAATTGTAAGGGTGACCTGGTTGAGTTTAAGCCTACTATT ATGATCGGTGTGGCTGCCGTTTGGGAAACTGTGAGAAAAGCTATTTTGGAAAAGATCAGC GATTTAACTCCCGTACTCCAAAAGATTTTTTGGTCTGCCTATAGTATGAAAGAAAAGAGT GTACCATGCACCGGGTTTTTAAGTCGTATGGTCTTCAAGAAAGTCAGACAAGCCACCGGT GGTCATCTTAAGTATATTATGAACGGTGGGTCTGCGATCAGTATTGATGCTCAGAAATTC TTTTCTATCGTCCTGTGTCCTATGATTATCGGTTACGGCCTTACTGAAACAGTTGCGAAT GCTTGTGTTTTGGAGCCTGATCATTTCGAATATGGTATAGTTGGTGATCTTGTTGGATCG GTCACTGCCAAATTGGTGGATGTTAAGGACCTAGGTTATTATGCAAAAAACAATCAAGGT GAATTGCTTCTAAAGGGTGCGCCGGTCTGTTCTGAATATTATAAGAATCCAATAGAAACG GCGGTCTCTTTCACTTACGATGGATGGTTTCGTACTGGTGATATTGTTGAATGGACTCCC AAGGGACAACTTAAAATTATTGATAGAAGAAAGAATTTGGTTAAAACCCTAAATGGTGAA TATATTGCATTAGAAAAGTTAGAATCTGTTTACAGGTCAAACTCCTATGTGAAAAATATC TGTGTTTATGCCGATGAAAGTAGGGTTAAACCGGTGGGTATTGTGGTACCCAACCCAGGA CCCCTATCTAAATTTGCTGTCAAATTGCGTATTATGAAAAAGGGTGAAGACATCGAAAAC TATATCCATGACAAAGCATTACGAAATGCTGTTTTCAAAGAGATGATCGCAACAGCCAAA TCTCAAGGTTTGGTTGGTATTGAACTATTATGTGGTATTGTTTTCTTTGATGAAGAATGG ACACCTGAAAATGGCTTTGTCACATCTGCTCAAAAATTAAAGAGAAGAGAAATCTTAGCC GCTGTTAAATCAGAAGTCGAAAGGGTTTACAAAGAAAATTCTTAG
Protein Properties
Pfam Domain Function
Protein Residues694
Protein Molecular Weight77946.0
Protein Theoretical pI9.41
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Long-chain-fatty-acid--CoA ligase 3 MSEQHSVAVGKAANEHETAPRRNVRVKKRPLIRPLNSSASTLYEFALECFNKGGKRDGMA WRDVIEIHETKKTIVRKVDGKDKSIEKTWLYYEMSPYKMMTYQELIWVMHDMGRGLAKIG IKPNGEHKFHIFASTSHKWMKIFLGCISQGIPVVTAYDTLGESGLIHSMVETESAAIFTD NQLLAKMIVPLQSAKDIKFLIHNEPIDPNDRRQNGKLYKAAKDAINKIREVRPDIKIYSF EEVVKIGKKSKDEVKLHPPEPKDLACIMYTSGSISAPKGVVLTHYNIVSGIAGVGHNVFG WIGSTDRVLSFLPLAHIFELVFEFEAFYWNGILGYGSVKTLTNTSTRNCKGDLVEFKPTI MIGVAAVWETVRKAILEKISDLTPVLQKIFWSAYSMKEKSVPCTGFLSRMVFKKVRQATG GHLKYIMNGGSAISIDAQKFFSIVLCPMIIGYGLTETVANACVLEPDHFEYGIVGDLVGS VTAKLVDVKDLGYYAKNNQGELLLKGAPVCSEYYKNPIETAVSFTYDGWFRTGDIVEWTP KGQLKIIDRRKNLVKTLNGEYIALEKLESVYRSNSYVKNICVYADESRVKPVGIVVPNPG PLSKFAVKLRIMKKGEDIENYIHDKALRNAVFKEMIATAKSQGLVGIELLCGIVFFDEEW TPENGFVTSAQKLKRREILAAVKSEVERVYKENS
References
External Links
ResourceLink
Saccharomyces Genome Database FAA3
Uniprot IDP39002
Uniprot NameLCF3_YEAST
GenBank Gene IDAY558110
Genebank Protein ID45270110
General Reference
  • Johnson, D. R., Knoll, L. J., Rowley, N., Gordon, J. I. (1994). "Genetic analysis of the role of Saccharomyces cerevisiae acyl-CoA synthetase genes in regulating protein N-myristoylation." J Biol Chem 269:18037-18046.8027063
  • 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
  • Knoll, L. J., Johnson, D. R., Gordon, J. I. (1994). "Biochemical studies of three Saccharomyces cerevisiae acyl-CoA synthetases, Faa1p, Faa2p, and Faa3p." J Biol Chem 269:16348-16356.8206942
  • 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