Long-chain-fatty-acid--CoA ligase 2 (P39518)

Identification
NameLong-chain-fatty-acid--CoA ligase 2
Synonyms
  • Fatty acid activator 2
  • Long-chain acyl-CoA synthetase 2
Gene NameFAA2
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. Preferentially acts on C9:0-C13:0 fatty acids although C7:0-C17:0 fatty acids are tolerated
Cellular LocationCytoplasm. Mitochondrion.
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
capric acid + Adenosine triphosphate + Coenzyme A ↔ Adenosine monophosphate + Pyrophosphate + decanoyl-CoA
lauric acid + Adenosine triphosphate + Coenzyme A ↔ Adenosine monophosphate + Pyrophosphate + lauroyl-CoA
Adenosine triphosphate + Coenzyme A + Palmitic acid ↔ Adenosine monophosphate + Pyrophosphate + Palmityl-CoA
Adenosine triphosphate + Coenzyme A + palmitoleic acid ↔ Adenosine monophosphate + Pyrophosphate + hexadec-2-enoyl-CoA
Adenosine triphosphate + Caprylic acid + Coenzyme A ↔ Adenosine monophosphate + Pyrophosphate + octanoyl-CoA
Metabolites
YMDB IDNameView
YMDB00045Coenzyme AShow
YMDB00069Palmitic acidShow
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00301Palmityl-CoAShow
YMDB00469hexadec-2-enoyl-CoAShow
YMDB00527palmitoyl-CoAShow
YMDB00528myristoyl-CoAShow
YMDB00530lauroyl-CoAShow
YMDB00531octanoyl-CoAShow
YMDB00532decanoyl-CoAShow
YMDB00676Caprylic acidShow
YMDB00677capric acidShow
YMDB00678lauric acidShow
YMDB00679myristic acidShow
YMDB00680Myristoleic acidShow
YMDB00681palmitoleic acidShow
GO Classification
Component
Not Available
Function
catalytic activity
Process
metabolic process
Gene Properties
Chromosome Locationchromosome 5
LocusYER015W
Gene Sequence>2235 bp ATGGCCGCTCCAGATTATGCACTTACCGATTTAATTGAATCGGATCCTCGTTTCGAAAGT TTGAAGACAAGATTAGCCGGTTACACCAAAGGCTCTGATGAATATATTGAAGAGCTATAC TCTCAATTACCACTGACCAGCTATCCCAGGTACAAAACATTTTTAAAGAAACAGGCGGTT GCCATTTCGAATCCGGATAATGAAGCTGGTTTTAGCTCGATTTATAGGAGTTCTCTTTCT TCTGAAAATCTAGTGAGCTGTGTGGATAAAAACTTAAGAACTGCATACGATCACTTCATG TTTTCTGCAAGGAGATGGCCTCAACGTGACTGTTTAGGTTCAAGGCCAATTGATAAAGCC ACAGGCACCTGGGAGGAAACATTCCGTTTCGAGTCGTACTCCACGGTATCTAAAAGATGT CATAATATCGGAAGTGGTATATTGTCTTTGGTAAACACGAAAAGGAAACGTCCTTTGGAA GCCAATGATTTTGTTGTTGCTATCTTATCACACAACAACCCTGAATGGATCCTAACAGAT TTGGCCTGTCAGGCCTATTCTCTAACTAACACGGCTTTGTACGAAACATTAGGTCCAAAC ACCTCCGAGTACATATTGAATTTAACCGAGGCCCCCATTCTGATTTTTGCAAAATCAAAT ATGTATCATGTATTGAAGATGGTGCCTGATATGAAATTTGTTAATACTTTGGTTTGTATG GATGAATTAACTCATGACGAGCTCCGTATGCTAAATGAATCGTTGCTACCCGTTAAGTGC AACTCTCTCAATGAAAAAATCACATTTTTTTCATTGGAGCAGGTAGAACAAGTTGGTTGC TTTAACAAAATTCCTGCAATTCCACCTACCCCAGATTCCTTGTATACTATTTCGTTTACT TCTGGTACTACAGGTTTACCTAAAGGTGTGGAAATGTCTCACAGAAACATTGCGTCTGGG ATAGCATTTGCTTTTTCTACCTTCAGAATACCGCCAGATAAAAGAAACCAACAGTTATAT GATATGTGTTTTTTGCCATTGGCTCATATTTTTGAAAGAATGGTTATTGCGTATGATCTA GCCATCGGGTTTGGAATAGGCTTCTTACATAAACCAGACCCAACTGTATTGGTAGAGGAT TTGAAGATTTTGAAACCTTACGCGGTTGCCCTGGTTCCTAGAATATTAACACGGTTTGAA GCCGGTATAAAAAACGCTTTGGATAAATCGACTGTCCAGAGGAACGTAGCAAATACTATA TTGGATTCTAAATCGGCCAGATTTACCGCAAGAGGTGGTCCAGATAAATCGATTATGAAT TTTCTAGTTTATCATCGCGTATTGATTGATAAAATCAGAGACTCTTTAGGTTTGTCCAAT AACTCGTTTATAATTACCGGATCAGCTCCCATATCTAAAGATACCTTACTATTTTTAAGA AGTGCCTTGGATATTGGTATAAGACAGGGCTACGGCTTAACTGAAACTTTTGCTGGTGTC TGTTTAAGCGAACCGTTTGAAAAAGATGTCGGATCTTGTGGTGCCATAGGTATTTCTGCA GAATGTAGATTGAAGTCTGTTCCAGAAATGGGTTACCATGCCGACAAGGATTTAAAAGGT GAACTGCAAATTCGTGGCCCACAGGTTTTTGAAAGATATTTTAAAAATCCGAATGAAACT TCAAAAGCCGTTGACCAAGATGGTTGGTTTTCCACGGGAGATGTTGCATTTATCGATGGA AAAGGTCGCATCAGCGTCATTGATCGAGTCAAGAACTTTTTCAAGCTAGCACATGGTGAA TATATTGCTCCAGAGAAAATCGAAAATATTTATTTATCATCATGCCCCTATATCACGCAA ATATTTGTCTTTGGAGATCCTTTAAAGACATTTTTAGTTGGCATCGTTGGTGTTGATGTT GATGCAGCGCAACCGATTTTAGCTGCAAAGCACCCAGAGGTGAAAACGTGGACTAAGGAA GTGCTAGTAGAAAACTTAAATCGTAATAAAAAGCTAAGGAAGGAATTTTTAAACAAAATT AATAAATGCACCGATGGGCTACAAGGATTCGAAAAATTGCATAACATCAAAGTCGGACTT GAGCCTTTAACTCTCGAGGATGATGTTGTGACGCCAACTTTTAAAATAAAGCGTGCCAAA GCATCAAAATTCTTCAAAGATACATTAGACCAACTATACGCCGAAGGTTCACTAGTCAAG ACAGAAAAGCTTTAG
Protein Properties
Pfam Domain Function
Protein Residues744
Protein Molecular Weight83437.10156
Protein Theoretical pI7.82
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Long-chain-fatty-acid--CoA ligase 2 MAAPDYALTDLIESDPRFESLKTRLAGYTKGSDEYIEELYSQLPLTSYPRYKTFLKKQAV AISNPDNEAGFSSIYRSSLSSENLVSCVDKNLRTAYDHFMFSARRWPQRDCLGSRPIDKA TGTWEETFRFESYSTVSKRCHNIGSGILSLVNTKRKRPLEANDFVVAILSHNNPEWILTD LACQAYSLTNTALYETLGPNTSEYILNLTEAPILIFAKSNMYHVLKMVPDMKFVNTLVCM DELTHDELRMLNESLLPVKCNSLNEKITFFSLEQVEQVGCFNKIPAIPPTPDSLYTISFT SGTTGLPKGVEMSHRNIASGIAFAFSTFRIPPDKRNQQLYDMCFLPLAHIFERMVIAYDL AIGFGIGFLHKPDPTVLVEDLKILKPYAVALVPRILTRFEAGIKNALDKSTVQRNVANTI LDSKSARFTARGGPDKSIMNFLVYHRVLIDKIRDSLGLSNNSFIITGSAPISKDTLLFLR SALDIGIRQGYGLTETFAGVCLSEPFEKDVGSCGAIGISAECRLKSVPEMGYHADKDLKG ELQIRGPQVFERYFKNPNETSKAVDQDGWFSTGDVAFIDGKGRISVIDRVKNFFKLAHGE YIAPEKIENIYLSSCPYITQIFVFGDPLKTFLVGIVGVDVDAAQPILAAKHPEVKTWTKE VLVENLNRNKKLRKEFLNKINKCTDGLQGFEKLHNIKVGLEPLTLEDDVVTPTFKIKRAK ASKFFKDTLDQLYAEGSLVKTEKL
References
External Links
ResourceLink
Saccharomyces Genome Database FAA2
Uniprot IDP39518
Uniprot NameLCF2_YEAST
GenBank Gene IDU18778
Genebank Protein ID603607
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
  • Harington, A., Schwarz, E., Slonimski, P. P., Herbert, C. J. (1994). "Subcellular relocalization of a long-chain fatty acid CoA ligase by a suppressor mutation alleviates a respiration deficiency in Saccharomyces cerevisiae." EMBO J 13:5531-5538.7988550
  • Dietrich, F. S., Mulligan, J., Hennessy, K., Yelton, M. A., Allen, E., Araujo, R., Aviles, E., Berno, A., Brennan, T., Carpenter, J., Chen, E., Cherry, J. M., Chung, E., Duncan, M., Guzman, E., Hartzell, G., Hunicke-Smith, S., Hyman, R. W., Kayser, A., Komp, C., Lashkari, D., Lew, H., Lin, D., Mosedale, D., Davis, R. W., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Nature 387:78-81.9169868
  • 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
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956