LCF1_YEAST
ID LCF1_YEAST Reviewed; 700 AA.
AC P30624; D6W316;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 1;
DE EC=6.2.1.3 {ECO:0000269|PubMed:8206942};
DE AltName: Full=Fatty acid activator 1;
DE AltName: Full=Fatty acyl-CoA synthetase;
DE Short=ACS;
DE Short=FACS;
DE AltName: Full=Long-chain acyl-CoA synthetase 1;
GN Name=FAA1; OrderedLocusNames=YOR317W; ORFNames=O6136;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 4-14.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1572893; DOI=10.1083/jcb.117.3.515;
RA Duronio R.J., Knoll L.J., Gordon J.I.;
RT "Isolation of a Saccharomyces cerevisiae long chain fatty acyl:CoA
RT synthetase gene (FAA1) and assessment of its role in protein N-
RT myristoylation.";
RL J. Cell Biol. 117:515-529(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896266;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA Schweizer M.;
RT "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT XV reveals regions of similarity to chromosomes I and XIII.";
RL Yeast 12:1021-1031(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8206942; DOI=10.1016/s0021-9258(17)34014-0;
RA Knoll L.J., Johnson D.R., Gordon J.I.;
RT "Biochemical studies of three Saccharomyces cerevisiae acyl-CoA
RT synthetases, Faa1p, Faa2p, and Faa3p.";
RL J. Biol. Chem. 269:16348-16356(1994).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10515935; DOI=10.1128/jb.181.20.6441-6448.1999;
RA Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., Daum G.;
RT "Identification and characterization of major lipid particle proteins of
RT the yeast Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:6441-6448(1999).
RN [7]
RP FUNCTION.
RX PubMed=11477098; DOI=10.1074/jbc.m100884200;
RA Faergeman N.J., Black P.N., Zhao X.D., Knudsen J., DiRusso C.C.;
RT "The acyl-CoA synthetases encoded within FAA1 and FAA4 in Saccharomyces
RT cerevisiae function as components of the fatty acid transport system
RT linking import, activation, and intracellular utilization.";
RL J. Biol. Chem. 276:37051-37059(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH FAT1.
RX PubMed=12601005; DOI=10.1074/jbc.m210557200;
RA Zou Z., Tong F., Faergeman N.J., Boersting C., Black P.N., DiRusso C.C.;
RT "Vectorial acylation in Saccharomyces cerevisiae. Fat1p and fatty acyl-CoA
RT synthetase are interacting components of a fatty acid import complex.";
RL J. Biol. Chem. 278:16414-16422(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=21820081; DOI=10.1016/j.bbalip.2011.07.015;
RA Grillitsch K., Connerth M., Kofeler H., Arrey T.N., Rietschel B.,
RA Wagner B., Karas M., Daum G.;
RT "Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited:
RT lipidome meets proteome.";
RL Biochim. Biophys. Acta 1811:1165-1176(2011).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22633490; DOI=10.1016/j.molcel.2012.04.033;
RA Nakahara K., Ohkuni A., Kitamura T., Abe K., Naganuma T., Ohno Y.,
RA Zoeller R.A., Kihara A.;
RT "The Sjogren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of
RT the sphingosine 1-phosphate degradation pathway.";
RL Mol. Cell 46:461-471(2012).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [15]
RP CATALYTIC ACTIVITY.
RX PubMed=24269233; DOI=10.1016/j.bbrc.2013.11.036;
RA Ohkuni A., Ohno Y., Kihara A.;
RT "Identification of acyl-CoA synthetases involved in the mammalian
RT sphingosine 1-phosphate metabolic pathway.";
RL Biochem. Biophys. Res. Commun. 442:195-201(2013).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=24868093; DOI=10.1194/jlr.m050229;
RA Currie E., Guo X., Christiano R., Chitraju C., Kory N., Harrison K.,
RA Haas J., Walther T.C., Farese R.V. Jr.;
RT "High-confidence proteomic analysis of yeast lipid droplets identifies
RT additional droplet proteins and reveals connections to dolichol synthesis
RT and sterol acetylation.";
RL J. Lipid Res. 55:1465-1477(2014).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-271 AND ASP-538, AND
RP DOMAIN.
RX PubMed=27136724; DOI=10.1038/srep25469;
RA Narita T., Naganuma T., Sase Y., Kihara A.;
RT "Long-chain bases of sphingolipids are transported into cells via the acyl-
RT CoA synthetases.";
RL Sci. Rep. 6:25469-25469(2016).
CC -!- FUNCTION: Activates long-chain fatty acids (LCFA) by esterification of
CC the fatty acids into metabolically active CoA-thioesters for subsequent
CC degradation or incorporation into phospholipids. Also facilitates the
CC transport of LCFAs into the cell, either by active transport or by
CC decreasing the intracellular LCFA concentration (PubMed:8206942,
CC PubMed:11477098, PubMed:12601005, PubMed:27136724). It may supplement
CC intracellular myristoyl-CoA pools from exogenous myristate.
CC Preferentially acts on C12:0-C16:0 fatty acids with myristic and
CC pentadecanic acid (C15:0) having the highest activities
CC (PubMed:8206942). Also involved in long-chain base (LCB) uptake of
CC sphingolipids. In contrast ot LCFA uptake, LCB uptake does not require
CC ATP, suggesting that the enzyme is directly involved in active LCB
CC uptake (PubMed:27136724). Involved in the sphingolipid-to-glycerolipid
CC metabolic pathway, converting the shingolipid metabolite hexadecenoic
CC acid to hexadecenoyl-CoA, which is then further converted to
CC glycerolipids (PubMed:22633490). {ECO:0000269|PubMed:11477098,
CC ECO:0000269|PubMed:12601005, ECO:0000269|PubMed:22633490,
CC ECO:0000269|PubMed:27136724, ECO:0000269|PubMed:8206942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:11477098, ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000305|PubMed:11477098, ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22633490,
CC ECO:0000269|PubMed:24269233, ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000305|PubMed:22633490, ECO:0000305|PubMed:24269233,
CC ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoate + ATP + CoA = (9Z)-hexadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33647, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:11477098, ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33648;
CC Evidence={ECO:0000305|PubMed:11477098, ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoate + ATP + CoA = (9Z)-tetradecenoyl-CoA + AMP
CC + diphosphate; Xref=Rhea:RHEA:33643, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32370, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65060, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33644;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + pentadecanoate = AMP + diphosphate +
CC pentadecanoyl-CoA; Xref=Rhea:RHEA:44076, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309,
CC ChEBI:CHEBI:78795, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44077;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + undecanoate = AMP + diphosphate + undecanoyl-CoA;
CC Xref=Rhea:RHEA:44080, ChEBI:CHEBI:30616, ChEBI:CHEBI:32369,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:77547,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44081;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + heptadecanoate = AMP + diphosphate +
CC heptadecanoyl-CoA; Xref=Rhea:RHEA:44084, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32366, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:74307, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44085;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octadecanoate = AMP + diphosphate + octadecanoyl-
CC CoA; Xref=Rhea:RHEA:33615, ChEBI:CHEBI:25629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8206942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616;
CC Evidence={ECO:0000305|PubMed:8206942};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8206942};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for myristate {ECO:0000269|PubMed:8206942};
CC KM=23 uM for palmitate {ECO:0000269|PubMed:8206942};
CC Vmax=83 pmol/min/mg enzyme for myristate
CC {ECO:0000269|PubMed:8206942};
CC Vmax=250 pmol/min/mg enzyme for palmitate
CC {ECO:0000269|PubMed:8206942};
CC pH dependence:
CC Optimum pH is 7.3-7.5. {ECO:0000269|PubMed:8206942};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:8206942};
CC -!- SUBUNIT: Interacts with FAT1. {ECO:0000269|PubMed:12601005}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935,
CC ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}. Cell
CC membrane {ECO:0000269|PubMed:27136724}.
CC -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC specificity. {ECO:0000305|PubMed:27136724}.
CC -!- MISCELLANEOUS: Present with 7470 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; X66194; CAA46957.1; -; Genomic_DNA.
DR EMBL; X90565; CAA62172.1; -; Genomic_DNA.
DR EMBL; Z75225; CAA99637.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11082.1; -; Genomic_DNA.
DR PIR; S23052; S23052.
DR RefSeq; NP_014962.3; NM_001183737.3.
DR AlphaFoldDB; P30624; -.
DR SMR; P30624; -.
DR BioGRID; 34704; 155.
DR DIP; DIP-4654N; -.
DR IntAct; P30624; 7.
DR STRING; 4932.YOR317W; -.
DR SwissLipids; SLP:000000132; -.
DR CarbonylDB; P30624; -.
DR iPTMnet; P30624; -.
DR MaxQB; P30624; -.
DR PaxDb; P30624; -.
DR PRIDE; P30624; -.
DR EnsemblFungi; YOR317W_mRNA; YOR317W; YOR317W.
DR GeneID; 854495; -.
DR KEGG; sce:YOR317W; -.
DR SGD; S000005844; FAA1.
DR VEuPathDB; FungiDB:YOR317W; -.
DR eggNOG; KOG1180; Eukaryota.
DR GeneTree; ENSGT00940000171609; -.
DR HOGENOM; CLU_000022_45_2_1; -.
DR InParanoid; P30624; -.
DR OMA; GEGEKMP; -.
DR BioCyc; YEAST:YOR317W-MON; -.
DR Reactome; R-SCE-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-SCE-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR PRO; PR:P30624; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P30624; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:SGD.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IDA:SGD.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IMP:SGD.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IMP:SGD.
DR GO; GO:1905329; P:sphingoid long-chain base transport; IMP:SGD.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Direct protein sequencing;
KW Fatty acid metabolism; Isopeptide bond; Ligase; Lipid droplet;
KW Lipid metabolism; Magnesium; Membrane; Nucleotide-binding;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..700
FT /note="Long-chain-fatty-acid--CoA ligase 1"
FT /id="PRO_0000193119"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 531..580
FT /note="FACS"
FT /evidence="ECO:0000305|PubMed:27136724"
FT BINDING 269..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69451"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 271
FT /note="S->A: Likely essential for ATP utilization. Reduces
FT catalytic activity by 89%. Reduces the LCA palmitic acid
FT transport activity by 71%. has no effect on the LCB
FT dihydrosphingosine (DHS) transport activity."
FT /evidence="ECO:0000269|PubMed:27136724"
FT MUTAGEN 538
FT /note="D->A: Abolishes catalytic activity. Reduces the LCA
FT palmitic acid transport activity by 96%. Abolishes the LCB
FT dihydrosphingosine (DHS) transport activity."
FT /evidence="ECO:0000269|PubMed:27136724"
SQ SEQUENCE 700 AA; 77866 MW; 56EE7E04D95BC5C9 CRC64;
MVAQYTVPVG KAANEHETAP RRNYQCREKP LVRPPNTKCS TVYEFVLECF QKNKNSNAMG
WRDVKEIHEE SKSVMKKVDG KETSVEKKWM YYELSHYHYN SFDQLTDIMH EIGRGLVKIG
LKPNDDDKLH LYAATSHKWM KMFLGAQSQG IPVVTAYDTL GEKGLIHSLV QTGSKAIFTD
NSLLPSLIKP VQAAQDVKYI IHFDSISSED RRQSGKIYQS AHDAINRIKE VRPDIKTFSF
DDILKLGKES CNEIDVHPPG KDDLCCIMYT SGSTGEPKGV VLKHSNVVAG VGGASLNVLK
FVGNTDRVIC FLPLAHIFEL VFELLSFYWG ACIGYATVKT LTSSSVRNCQ GDLQEFKPTI
MVGVAAVWET VRKGILNQID NLPFLTKKIF WTAYNTKLNM QRLHIPGGGA LGNLVFKKIR
TATGGQLRYL LNGGSPISRD AQEFITNLIC PMLIGYGLTE TCASTTILDP ANFELGVAGD
LTGCVTVKLV DVEELGYFAK NNQGEVWITG ANVTPEYYKN EEETSQALTS DGWFKTGDIG
EWEANGHLKI IDRKKNLVKT MNGEYIALEK LESVYRSNEY VANICVYADQ SKTKPVGIIV
PNHAPLTKLA KKLGIMEQKD SSINIENYLE DAKLIKAVYS DLLKTGKDQG LVGIELLAGI
VFFDGEWTPQ NGFVTSAQKL KRKDILNAVK DKVDAVYSSS
