PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
30929440-3	2019	Through disruption of the acyl-CoA synthetases FAA1 and FAA4 and the fatty acyl-CoA oxidase POX1, a Saccharomyces cerevisiae strain was engineered to accumulate free fatty acids (FFAs).	Fatty Acids, Nonesterified	161-177	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	47-51
8440712-11	1993	Faa1p can also rescue growth at 37 degrees C of fadD- strains on minimal media supplemented with C12:0, although this rescue becomes less efficient as the chain length of the supplemental fatty acid increases.	Fatty Acids	188-198	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	0-5
8440712-12	1993	In addition, S. cerevisiae Faa1p is better able to direct myristoyl-CoA to the bacteria"s phospholipid biosynthetic pathways than FadD, while FadD is more efficient at directing myristoyl-CoA to the genetically engineered protein N-myristoylation pathway.	S-tetradecanoyl-coenzyme A	58-71	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	27-32
8440712-12	1993	In addition, S. cerevisiae Faa1p is better able to direct myristoyl-CoA to the bacteria"s phospholipid biosynthetic pathways than FadD, while FadD is more efficient at directing myristoyl-CoA to the genetically engineered protein N-myristoylation pathway.	Phospholipids	90-102	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	27-32
8440712-12	1993	In addition, S. cerevisiae Faa1p is better able to direct myristoyl-CoA to the bacteria"s phospholipid biosynthetic pathways than FadD, while FadD is more efficient at directing myristoyl-CoA to the genetically engineered protein N-myristoylation pathway.	S-tetradecanoyl-coenzyme A	178-191	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	27-32
8440712-12	1993	In addition, S. cerevisiae Faa1p is better able to direct myristoyl-CoA to the bacteria"s phospholipid biosynthetic pathways than FadD, while FadD is more efficient at directing myristoyl-CoA to the genetically engineered protein N-myristoylation pathway.	Nitrogen	230-231	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	27-32
1572893-3	1992	The FAA1 (fatty acid activation) gene has been isolated by genetic complementation of a faal mutant.	Fatty Acids	10-20	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	4-8
1572893-7	1992	At 36 degrees C, FAA1 is required for the utilization of exogenous myristate by NMT and for the synthesis of several phospholipid species.	Phospholipids	117-129	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	17-21
18422644-3	2008	The combined deletion of Faa1p and Faa4p encoding two out of five acyl-CoA synthetases was necessary and sufficient to establish mutant cells that secreted fatty acids in a growth-phase dependent manner.	Fatty Acids	156-167	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	25-30
18422644-9	2008	Therefore, we propose the recycling of endogenous fatty acids generated in the course of lipid remodelling as a major task of both acyl-CoA synthetases Faa1p and Faa4p.	Fatty Acids	50-61	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	152-157
35081466-0	2022	A homologue of yeast acyl-CoA synthetase Faa1 contributes to cytomembrane functionality involved in development and virulence in the insect pathogenic fungus Beauveria bassiana.	cytomembrane	61-73	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	41-45
35081466-7	2022	Our findings indicate that the metabolism of acyl-CoA synthetase Faa1 contributes to the cytomembrane functionality which cascades hydrophobin translocation and differentiation, thus affecting virulence of B. bassiana.	cytomembrane	89-101	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	65-69
31546626-3	2019	To clarify the mechanism of LCFA acquisition, we investigated fatty acid uptake by this fungus and identified the long-chain acyl-CoA synthetase (ACS) gene FAA1 in three Malassezia spp.	Acyl Coenzyme A	125-133	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	156-160
31546626-7	2019	Interestingly, the ACS inhibitor, triacsin C, affected the activity of the Malassezia Faa1 proteins but not that of S. cerevisiae.	triacsin C	34-44	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	86-90
26019148-3	2015	The FAT1 deletion mutant exhibited decreased growth on n-alkanes of 10-18 carbons, whereas the FAA1 mutant showed growth reduction on n-alkane of 16 carbons.	Carbon	149-156	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	95-99
26019148-4	2015	However, FAT2-FAT4 deletion mutants did not show any growth defects, suggesting that FAT1 and FAA1 are involved in the activation of fatty acids produced during the metabolism of n-alkanes.	Fatty Acids	133-144	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	94-98
26019148-4	2015	However, FAT2-FAT4 deletion mutants did not show any growth defects, suggesting that FAT1 and FAA1 are involved in the activation of fatty acids produced during the metabolism of n-alkanes.	n-alkanes	179-188	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	94-98
26019148-7	2015	However, the FAA1 deletion mutant did not grow, indicating a critical role for FAA1 in the utilization of fatty acids.	Fatty Acids	106-117	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	13-17
26019148-7	2015	However, the FAA1 deletion mutant did not grow, indicating a critical role for FAA1 in the utilization of fatty acids.	Fatty Acids	106-117	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	79-83
30023691-4	2017	The FAA1 and FAA4 genes encoding two acyl-CoA synthetases in S. cerevisiae were deleted, resulting in the accumulation of FFAs with carbon chain length from C8 to C18.	Carbon	132-138	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	4-8
29163455-4	2017	Furthermore, the deletion of fatty acyl-CoA synthetase genes FAA1 and FAA4 increased the production of medium-chain alpha, omega-DCAs from 4.690 +- 0.088 mg/L to 12.177 +- 0.420 mg/L and enabled the production of C14 and C16 alpha, omega-DCAs at low percentage.	omega-dcas	123-133	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	61-65
22633490-5	2012	Moreover, we demonstrate that yeast Faa1 and Faa4 and mammalian ACSL family members are acyl-CoA synthetases involved in the sphingolipid-to-glycerolipid metabolic pathway and that hexadecenoic acid accumulates in Deltafaa1 Deltafaa4 mutant cells.	Sphingolipids	125-137	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	36-40
28298234-2	2017	Deletion of the fatty acyl-CoA synthetase genes FAA1 and FAA4 is an effective and straightforward way to disable re-activation of fatty acids and drastically increase FFA levels.	Fatty Acids	130-141	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	48-52
28298234-4	2017	In the present study, we aimed for dynamic expression of the fatty acyl-CoA synthetase gene FAA1 to regulate FFA and acyl-CoA pools in order to improve fatty alcohol production yields.	Fatty Alcohols	152-165	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	92-96
28298234-8	2017	Then, we expressed FAA1 under the control of different promoters in order to balance FFA and acyl-CoA interconversion rates and to achieve optimal levels for conversion to fatty alcohols.	Fatty Alcohols	172-186	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	19-23
28298234-9	2017	Expressing FAA1 under control of the HXT1 promoter led to an increased accumulation of fatty alcohols per OD600 up to 41% while FFA levels were decreased by 63% compared with the control strain.	Fatty Alcohols	87-101	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	11-15
26450510-1	2016	The engineered Saccharomyces cerevisiae strain  faa1 faa4 [Acot5s] was demonstrated to accumulate more free fatty acids (FFA) previously.	Fatty Acids, Nonesterified	103-119	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	48-57
26450510-4	2016	Proteins involved in glycolysis, acetate metabolism, fatty acid synthesis, TCA cycle, glyoxylate cycle, the pentose phosphate pathway, respiration, transportation, and stress response were found to be upregulated in  faa1 faa4 [Acot5s] as compared to the wild type.	Acetates	33-40	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	217-226
26450510-4	2016	Proteins involved in glycolysis, acetate metabolism, fatty acid synthesis, TCA cycle, glyoxylate cycle, the pentose phosphate pathway, respiration, transportation, and stress response were found to be upregulated in  faa1 faa4 [Acot5s] as compared to the wild type.	Fatty Acids	53-63	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	217-226
26450510-4	2016	Proteins involved in glycolysis, acetate metabolism, fatty acid synthesis, TCA cycle, glyoxylate cycle, the pentose phosphate pathway, respiration, transportation, and stress response were found to be upregulated in  faa1 faa4 [Acot5s] as compared to the wild type.	Trichloroacetic Acid	75-78	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	217-226
26450510-4	2016	Proteins involved in glycolysis, acetate metabolism, fatty acid synthesis, TCA cycle, glyoxylate cycle, the pentose phosphate pathway, respiration, transportation, and stress response were found to be upregulated in  faa1 faa4 [Acot5s] as compared to the wild type.	glyoxylic acid	86-96	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	217-226
26450510-4	2016	Proteins involved in glycolysis, acetate metabolism, fatty acid synthesis, TCA cycle, glyoxylate cycle, the pentose phosphate pathway, respiration, transportation, and stress response were found to be upregulated in  faa1 faa4 [Acot5s] as compared to the wild type.	Pentosephosphates	108-125	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	217-226
26450510-6	2016	Taken together with our metabolite analysis, our results showed that the disruption of Faa1 and Faa4 and expression of Acot5s in the engineered strain  faa1 faa4 [Acot5s] not only relieved the feedback inhibition of fatty acyl-CoAs on fatty acid synthesis, but also caused a major metabolic rearrangement.	Acyl Coenzyme A	216-231	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	87-91
26450510-6	2016	Taken together with our metabolite analysis, our results showed that the disruption of Faa1 and Faa4 and expression of Acot5s in the engineered strain  faa1 faa4 [Acot5s] not only relieved the feedback inhibition of fatty acyl-CoAs on fatty acid synthesis, but also caused a major metabolic rearrangement.	Acyl Coenzyme A	216-231	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	152-161
26450510-6	2016	Taken together with our metabolite analysis, our results showed that the disruption of Faa1 and Faa4 and expression of Acot5s in the engineered strain  faa1 faa4 [Acot5s] not only relieved the feedback inhibition of fatty acyl-CoAs on fatty acid synthesis, but also caused a major metabolic rearrangement.	Fatty Acids	235-245	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	87-91
26450510-6	2016	Taken together with our metabolite analysis, our results showed that the disruption of Faa1 and Faa4 and expression of Acot5s in the engineered strain  faa1 faa4 [Acot5s] not only relieved the feedback inhibition of fatty acyl-CoAs on fatty acid synthesis, but also caused a major metabolic rearrangement.	Fatty Acids	235-245	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	152-161
25461829-6	2015	Disruptions in the acyl-CoA synthetase genes FAA1, FAA4 and FAT1 allowed the extracellular detection of free fatty acids up to 490mg/L.	Fatty Acids, Nonesterified	104-120	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	45-49
24370880-0	2014	Enhanced ethyl caproate production of Chinese liquor yeast by overexpressing EHT1 with deleted FAA1.	ethyl hexanoate	9-23	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	95-99
24769906-6	2014	The resulting strain  faa1 faa4 [Acot5s] accumulated more extracellular FFA with higher unsaturated fatty acid (UFA) ratio as compared to the wild-type strain and double deletion strain  faa1 faa4.	Fatty Acids, Unsaturated	88-110	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	22-31
24769906-6	2014	The resulting strain  faa1 faa4 [Acot5s] accumulated more extracellular FFA with higher unsaturated fatty acid (UFA) ratio as compared to the wild-type strain and double deletion strain  faa1 faa4.	Fatty Acids, Unsaturated	112-115	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	22-31
24769906-7	2014	The extracellular total fatty acids (TFA) in the strain  faa1 faa4 [Acot5s] increased to 6.43-fold as compared to the wild-type strain during the stationary phase.	Fatty Acids	24-35	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	57-66
24769906-7	2014	The extracellular total fatty acids (TFA) in the strain  faa1 faa4 [Acot5s] increased to 6.43-fold as compared to the wild-type strain during the stationary phase.	Trifluoroacetic Acid	37-40	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	57-66
24769906-8	2014	UFA accounted for 42 % of TFA in the strain  faa1 faa4 [Acot5s], while no UFA was detected in the wild-type strain.	Fatty Acids, Unsaturated	0-3	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	45-54
22633490-5	2012	Moreover, we demonstrate that yeast Faa1 and Faa4 and mammalian ACSL family members are acyl-CoA synthetases involved in the sphingolipid-to-glycerolipid metabolic pathway and that hexadecenoic acid accumulates in Deltafaa1 Deltafaa4 mutant cells.	glycerolipid	141-153	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	36-40
22633490-5	2012	Moreover, we demonstrate that yeast Faa1 and Faa4 and mammalian ACSL family members are acyl-CoA synthetases involved in the sphingolipid-to-glycerolipid metabolic pathway and that hexadecenoic acid accumulates in Deltafaa1 Deltafaa4 mutant cells.	hexadecenoic acid	181-198	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	36-40
9988704-14	1999	Simultaneous disruption of FAA1 and FAA4, which encode long chain (C14-C18) fatty acyl-CoA synthetases, effectively blocks the import of long chain saturated and unsaturated fatty acids.	long chain saturated and unsaturated fatty acids	137-185	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	27-31
17604220-4	2007	Our previous work has shown Faa1p is a principal component of a fatty acid transport/activation complex that also includes the fatty acid transport protein Fat1p.	Fatty Acids	64-74	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	28-33
17604220-4	2007	Our previous work has shown Faa1p is a principal component of a fatty acid transport/activation complex that also includes the fatty acid transport protein Fat1p.	Fatty Acids	127-137	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	28-33
17604220-5	2007	In the present work hexameric histidine tagged Faa1p was purified to homogeneity through a two-step process in the presence of 0.1% eta-dodecyl-beta-maltoside following expression at 15 degrees C in Escherichia coli.	Histidine	30-39	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	47-52
17604220-6	2007	In order to further define the role of this enzyme in fatty acid transport-coupled activation (vectorial acylation), initial velocity kinetic studies were completed to define the kinetic parameters of Faa1p in response to the different substrates and to define mechanism.	Fatty Acids	54-64	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	201-206
17604220-7	2007	These studies showed Faa1p had a Vmax of 158.2 nmol/min/mg protein and a Km of 71.1 microM oleate.	Oleic Acid	91-97	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	21-26
11751830-7	2002	This acyl-CoA-independent TAG synthase utilizes DAG as an acceptor and free fatty acids as cosubstrates and occurs independently of the acyl-CoA synthases Faa1p to Faa4p.	Fatty Acids, Nonesterified	71-87	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	155-160
16233202-12	2002	On the contrary, disruption of faa1 led to faster growth in the presence of ethanol.	Ethanol	76-83	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	31-35
16233202-13	2002	These results suggest that Faa1p and Faa4p play reciprocal roles in regulating protein modification during growth in the presence of ethanol, since Faa1p and Faa4p both function to incorporate palmitic acid into phospholipids and neutral lipids.	Ethanol	133-140	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	27-32
16233202-13	2002	These results suggest that Faa1p and Faa4p play reciprocal roles in regulating protein modification during growth in the presence of ethanol, since Faa1p and Faa4p both function to incorporate palmitic acid into phospholipids and neutral lipids.	Ethanol	133-140	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	148-153
16233202-13	2002	These results suggest that Faa1p and Faa4p play reciprocal roles in regulating protein modification during growth in the presence of ethanol, since Faa1p and Faa4p both function to incorporate palmitic acid into phospholipids and neutral lipids.	Palmitic Acid	193-206	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	27-32
16233202-13	2002	These results suggest that Faa1p and Faa4p play reciprocal roles in regulating protein modification during growth in the presence of ethanol, since Faa1p and Faa4p both function to incorporate palmitic acid into phospholipids and neutral lipids.	Palmitic Acid	193-206	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	148-153
16233202-13	2002	These results suggest that Faa1p and Faa4p play reciprocal roles in regulating protein modification during growth in the presence of ethanol, since Faa1p and Faa4p both function to incorporate palmitic acid into phospholipids and neutral lipids.	Phospholipids	212-225	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	27-32
16233202-13	2002	These results suggest that Faa1p and Faa4p play reciprocal roles in regulating protein modification during growth in the presence of ethanol, since Faa1p and Faa4p both function to incorporate palmitic acid into phospholipids and neutral lipids.	Phospholipids	212-225	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	148-153
16233202-14	2002	Moreover, Northern hybridization analysis revealed that faa1 mRNA was expressed strongly in a laboratory strain, and weakly in the sake yeast strain K-7 which exhibited good growth in the presence of ethanol.	Ethanol	200-207	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	56-60
16233202-15	2002	The combination of the disruption of faa1 and exogenously supplied palmitic acid was highly effective for growth in the presence of ethanol even under the normal snc1 expression level, implying that activation of exogenous palmitic acid by Faa4p is of particular importance in growth in ethanol.	Ethanol	132-139	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	37-41
16233202-15	2002	The combination of the disruption of faa1 and exogenously supplied palmitic acid was highly effective for growth in the presence of ethanol even under the normal snc1 expression level, implying that activation of exogenous palmitic acid by Faa4p is of particular importance in growth in ethanol.	Palmitic Acid	223-236	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	37-41
16233202-15	2002	The combination of the disruption of faa1 and exogenously supplied palmitic acid was highly effective for growth in the presence of ethanol even under the normal snc1 expression level, implying that activation of exogenous palmitic acid by Faa4p is of particular importance in growth in ethanol.	Ethanol	287-294	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	37-41
16232807-0	2000	Effect of the FAA1 gene disruption of sake yeast on the accumulation of ethyl caproate in sake mash.	ethyl hexanoate	72-86	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	14-18
16232807-1	2000	Fatty acid activation gene (FAA1) in sake yeast Kyokai no.	Fatty Acids	0-10	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	28-32
16232807-4	2000	The disruptant for the FAA1 gene (K701deltafaa1) exhibited a reduced growth rate in a medium containing cerulenin and myristic acid or oleic acid compared with that of the parental strain (K701).	Cerulenin	104-113	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	23-27
16232807-4	2000	The disruptant for the FAA1 gene (K701deltafaa1) exhibited a reduced growth rate in a medium containing cerulenin and myristic acid or oleic acid compared with that of the parental strain (K701).	Myristic Acid	118-131	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	23-27
16232807-4	2000	The disruptant for the FAA1 gene (K701deltafaa1) exhibited a reduced growth rate in a medium containing cerulenin and myristic acid or oleic acid compared with that of the parental strain (K701).	Oleic Acid	135-145	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	23-27
16232807-6	2000	These results suggest that the FAA1 gene in sake yeast plays an important role in sake brewing and the accumulation of ethyl caproate.	ethyl hexanoate	119-133	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	31-35
20851956-9	2010	Indeed, the induction of FAA1 and EEB1, coding for a long-chain fatty acyl coenzyme A synthetase and an alcohol acyltransferase, respectively, suggests a detoxification pathway through the production of decanoate ethyl ester.	decanoate ethyl ester	203-224	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	25-29
17679730-1	2007	The fatty acid transport protein (FATP) Fat1p in the yeast Saccharomyces cerevisiae functions in concert with acyl-coenzyme A synthetase (ACSL; either Faa1p or Faa4p) in vectorial acylation, which couples the transport of exogenous fatty acids with activation to CoA thioesters.	Fatty Acids	4-14	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	151-156
17679730-1	2007	The fatty acid transport protein (FATP) Fat1p in the yeast Saccharomyces cerevisiae functions in concert with acyl-coenzyme A synthetase (ACSL; either Faa1p or Faa4p) in vectorial acylation, which couples the transport of exogenous fatty acids with activation to CoA thioesters.	Fatty Acids	232-243	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	151-156
17679730-10	2007	This topological orientation is consistent with the mechanistic roles of both Fat1p and Faa1p or Faa4p in the coupled transport/activation of exogenous fatty acids by vectorial acylation.	Fatty Acids	152-163	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	88-93
16798075-5	2007	Pivotal roles have been defined for Faa1p and Faa4p in fatty acid import, beta-oxidation and transcriptional control mediated by the transcription factors Oaf1p/Pip2p and Mga2p/Spt23p.	Fatty Acids	55-65	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	36-41
12601005-14	2003	Collectively, these data support the hypothesis that fatty acid import by vectorial acylation in yeast requires a multiprotein complex, which consists of Fat1p and Faa1p or Faa4p.	Fatty Acids	53-63	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	164-169
16233436-4	2003	The mutation that causes the fatty acid secretion phenotype occurred at a single allele, and this phenotype was suppressed by the introduction of a single copy of FAA1, a gene for acyl-CoA Synthetase, to the mutant.	Fatty Acids	29-39	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	163-167
16233436-5	2003	Although the mutation expressing this phenotype was not within FAA1 in YTS51, the disruption of FAA1 in the wild-type strain resulted in fatty acid secretion even though the level of fatty acid secretion was less than that in YTS51.	Fatty Acids	137-147	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	96-100
16233436-5	2003	Although the mutation expressing this phenotype was not within FAA1 in YTS51, the disruption of FAA1 in the wild-type strain resulted in fatty acid secretion even though the level of fatty acid secretion was less than that in YTS51.	Fatty Acids	183-193	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	96-100
11477098-0	2001	The Acyl-CoA synthetases encoded within FAA1 and FAA4 in Saccharomyces cerevisiae function as components of the fatty acid transport system linking import, activation, and intracellular Utilization.	Fatty Acids	112-122	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	40-44
11477098-3	2001	Faa1p or Faa4p are essential for long-chain fatty acid import, suggesting that one or both of these enzymes are components of the fatty acid transport system, which also includes Fat1p.	long-chain fatty acid	33-54	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	0-5
11477098-3	2001	Faa1p or Faa4p are essential for long-chain fatty acid import, suggesting that one or both of these enzymes are components of the fatty acid transport system, which also includes Fat1p.	Fatty Acids	44-54	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	0-5
11477098-4	2001	By monitoring the intracellular accumulation of the fluorescent long-chain fatty acid analogue 4,4-difluoro-5-methyl-4-bora-3a,4a-diaza-s-indacene-3-dodecanoic acid, long-chain fatty acid transport was shown to be severely restricted in a faa1 Delta faa4 Delta strain.	long-chain fatty acid	64-85	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	239-243
11477098-4	2001	By monitoring the intracellular accumulation of the fluorescent long-chain fatty acid analogue 4,4-difluoro-5-methyl-4-bora-3a,4a-diaza-s-indacene-3-dodecanoic acid, long-chain fatty acid transport was shown to be severely restricted in a faa1 Delta faa4 Delta strain.	BODIPY-3823	95-164	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	239-243
11477098-7	2001	These studies demonstrated oleoyl CoA levels were reduced to less than 10% wild-type levels in faa1 Delta and faa1 Delta faa4 Delta strains.	Coenzyme A	34-37	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	95-131
11477098-11	2001	Northern analyses demonstrated an additional defect in fatty acid trafficking as FAA1 or FAA4 were required for the transcriptional regulation of the genes encoding the peroxisomal enzymes acyl-CoA oxidase (POX1) and medium-chain acyl-CoA synthetase (FAA2).	Fatty Acids	55-65	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	81-85
11477098-12	2001	These data support the hypothesis that fatty acyl-CoA synthetase (Faa1p or Faa4p) functions as a component of the fatty acid import system by linking import and activation of exogenous fatty acids to intracellular utilization and signaling.	Fatty Acids	114-124	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	66-71
11477098-12	2001	These data support the hypothesis that fatty acyl-CoA synthetase (Faa1p or Faa4p) functions as a component of the fatty acid import system by linking import and activation of exogenous fatty acids to intracellular utilization and signaling.	Fatty Acids	185-196	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	66-71
16233132-4	2001	AMPC16-induced events suggested that Faa1p, the major acyl-CoA synthetase isozyme, is functional for phospholipid reconstitution in the exponential growth phase.	adenosine 5'-hexadecylphosphate	0-6	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	37-42
16233132-4	2001	AMPC16-induced events suggested that Faa1p, the major acyl-CoA synthetase isozyme, is functional for phospholipid reconstitution in the exponential growth phase.	Phospholipids	101-113	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	37-42
9748261-2	1998	Faa1p and Faa4p activate exogenously derived fatty acids.	Fatty Acids	45-56	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	0-5
9748261-4	1998	In this report, we have examined whether Faa1p and Faa4p have distinct roles in affecting protein N-myristoylation as cells transition from growth in rich media to a growth-arrested state during nutrient deprivation (stationary phase).	Nitrogen	98-99	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	41-46
7738025-4	1995	The functionally interchangeable FAA1 and FAA4 genes are responsible for activation of these imported fatty acids.	Fatty Acids	102-113	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	33-37
9675816-9	1998	As has been reported for OLE1, the repression of ATF1 by unsaturated fatty acids was relieved in a disruptant carrying a faa1 and faa4 double mutation, two fatty acid activation genes.	Fatty Acids, Unsaturated	57-80	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	121-125
9675816-9	1998	As has been reported for OLE1, the repression of ATF1 by unsaturated fatty acids was relieved in a disruptant carrying a faa1 and faa4 double mutation, two fatty acid activation genes.	Fatty Acids	69-79	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	121-125
8631965-10	1996	Two fatty acid activation genes, FAA1 and FAA4, were found to be essential for unsaturated fatty acid repression of OLE1 through the FAR sequences.	Fatty Acids	4-14	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	33-37
8631965-10	1996	Two fatty acid activation genes, FAA1 and FAA4, were found to be essential for unsaturated fatty acid repression of OLE1 through the FAR sequences.	Fatty Acids, Unsaturated	79-101	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	33-37
7650027-3	1995	Recent genetic studies indicate that Faa1p and Faa4p are involved in the activation of imported fatty acids, while Faa2p activates endogenous pools of fatty acids.	Fatty Acids	96-107	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	37-42
7650027-6	1995	Surveys of C14 fatty acids with single cis-double bonds at C2-C12 indicated that Faa4p and Faa1p prefer Z9-tetradecenoic acid, although Faa4p"s preference is much greater and also evident in C16 and C18 fatty acids.	9-tetradecenoic acid	104-125	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	91-96
7650027-9	1995	Faa3p can only use E9-tetradecenoic acid as a substrate, while E4-, E6- and E9-tetradecenoic acids can be used by Faa1p and Faa2p.	e4-, e6- and e9-tetradecenoic acids	63-98	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	114-119
7738025-9	1995	Even though Faa1p, Faa4p, and RLACS are all able to activate imported myristate and palmitate in S. cerevisiae, the sensitivity of Faa4p and RLACS, but not Faa1p, to inhibition by triacsin C suggests that the rat liver enzyme is functionally more analogous to Faa4p than to Faa1p.	triacsin C	180-190	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	12-17
8027063-4	1994	We have isolated and characterized three unlinked Fatty Acid Activation genes from S. cerevisiae, FAA1, FAA2, and FAA3.	Fatty Acids	50-60	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	98-102
8206942-5	1994	In vitro assays of C3:0-C24:0 fatty acids indicate that Faa1p prefers C12:0-C16:0, with myristic and pentadecanoic acid (C15:0) having the highest activities.	Fatty Acids	30-41	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	56-61
8206942-5	1994	In vitro assays of C3:0-C24:0 fatty acids indicate that Faa1p prefers C12:0-C16:0, with myristic and pentadecanoic acid (C15:0) having the highest activities.	myristic and pentadecanoic acid	88-119	long-chain fatty acid-CoA ligase FAA1	Saccharomyces cerevisiae S288C	56-61