ID   LCF2_YEAST              Reviewed;         744 AA.
AC   P39518; D3DLR3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase 2;
DE            EC=6.2.1.3 {ECO:0000269|PubMed:8206942};
DE   AltName: Full=Fatty acid activator 2;
DE   AltName: Full=Long-chain acyl-CoA synthetase 2;
GN   Name=FAA2; Synonyms=FAM1; OrderedLocusNames=YER015W;
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].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8027063; DOI=10.1016/s0021-9258(17)32414-6;
RA   Johnson D.R., Knoll L.J., Rowley N., Gordon J.I.;
RT   "Genetic analysis of the role of Saccharomyces cerevisiae acyl-CoA
RT   synthetase genes in regulating protein N-myristoylation.";
RL   J. Biol. Chem. 269:18037-18046(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF MET-1, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=CW04;
RX   PubMed=7988550; DOI=10.1002/j.1460-2075.1994.tb06890.x;
RA   Harington A., Schwarz E., Slonimski P.P., Herbert C.J.;
RT   "Subcellular relocalization of a long-chain fatty acid CoA ligase by a
RT   suppressor mutation alleviates a respiration deficiency in Saccharomyces
RT   cerevisiae.";
RL   EMBO J. 13:5531-5538(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(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   INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8670886; DOI=10.1002/j.1460-2075.1996.tb00755.x;
RA   Hettema E.H., van Roermund C.W.T., Distel B., van den Berg M., Vilela C.,
RA   Rodrigues-Pousada C., Wanders R.J.A., Tabak H.F.;
RT   "The ABC transporter proteins Pat1 and Pat2 are required for import of
RT   long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae.";
RL   EMBO J. 15:3813-3822(1996).
RN   [7]
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   [8]
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   [9]
RP   FUNCTION.
RX   PubMed=22493507; DOI=10.1074/jbc.m111.332833;
RA   van Roermund C.W., Ijlst L., Majczak W., Waterham H.R., Folkerts H.,
RA   Wanders R.J., Hellingwerf K.J.;
RT   "Peroxisomal fatty acid uptake mechanism in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 287:20144-20153(2012).
RN   [10]
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).
CC   -!- FUNCTION: Activates endogenous medium-chain (MCFA) and long-chain fatty
CC       acids (LCFA) by esterification of the fatty acids into metabolically
CC       active CoA-thioesters for subsequent degradation or incorporation into
CC       phospholipids (PubMed:8206942). Preferentially acts on C9:0-C13:0 fatty
CC       acids although C7:0-C17:0 fatty acids are tolerated (PubMed:8206942).
CC       Is the main if not exclusive MCFA (octanoate, decanoate and laureate)
CC       acyl-CoA ligase. Required for efficient MCFA beta-oxidation inside
CC       peroxisomes. Facilitates the transport of MCFAs into peroxisomes by
CC       passive diffusion, by decreasing the intraorganellar MCFA concentration
CC       (PubMed:8670886). Also esterifies LCFAs in the peroxisome matrix. The
CC       LCFAs are actively transported into peroxisomes by a PXA1-PXA2
CC       heterodimeric transporter in the peroxisomal membrane
CC       (PubMed:22493507). {ECO:0000269|PubMed:22493507,
CC       ECO:0000269|PubMed:8206942, ECO:0000269|PubMed:8670886}.
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:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC         Evidence={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:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={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:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33648;
CC         Evidence={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 + decanoate = AMP + decanoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC         Evidence={ECO:0000305|PubMed:8206942};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC         Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC         Evidence={ECO:0000305|PubMed:8206942};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + heptanoate = AMP + diphosphate + heptanoyl-CoA;
CC         Xref=Rhea:RHEA:44088, ChEBI:CHEBI:30616, ChEBI:CHEBI:32362,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78811,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44089;
CC         Evidence={ECO:0000305|PubMed:8206942};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + nonadecanoate = AMP + diphosphate + nonadecanoyl-
CC         CoA; Xref=Rhea:RHEA:44092, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:75105, ChEBI:CHEBI:78796,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44093;
CC         Evidence={ECO:0000305|PubMed:8206942};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P30624};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.1. {ECO:0000269|PubMed:8206942};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:8206942};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7988550}.
CC       Peroxisome membrane {ECO:0000269|PubMed:8670886}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:8670886}; Matrix side
CC       {ECO:0000269|PubMed:8670886}. Note=Imported via the peroxisome
CC       targeting signal type 1 (PTS1)-dependent protein import pathway.
CC       {ECO:0000269|PubMed:8670886}.
CC   -!- INDUCTION: By oleate. {ECO:0000269|PubMed:8670886}.
CC   -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC       specificity. {ECO:0000250|UniProtKB:P30624}.
CC   -!- MISCELLANEOUS: Present with 358 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; X77783; CAA54817.1; -; Genomic_DNA.
DR   EMBL; X82364; CAA57780.1; -; Genomic_DNA.
DR   EMBL; U18778; AAB64548.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07667.1; -; Genomic_DNA.
DR   PIR; A54901; A54901.
DR   RefSeq; NP_010931.3; NM_001178906.3.
DR   AlphaFoldDB; P39518; -.
DR   SMR; P39518; -.
DR   BioGRID; 36747; 47.
DR   DIP; DIP-6565N; -.
DR   IntAct; P39518; 5.
DR   MINT; P39518; -.
DR   STRING; 4932.YER015W; -.
DR   SwissLipids; SLP:000001032; -.
DR   TCDB; 4.C.1.1.15; the fatty acid group translocation (fat) family.
DR   iPTMnet; P39518; -.
DR   MaxQB; P39518; -.
DR   PaxDb; 4932-YER015W; -.
DR   PeptideAtlas; P39518; -.
DR   EnsemblFungi; YER015W_mRNA; YER015W; YER015W.
DR   GeneID; 856734; -.
DR   KEGG; sce:YER015W; -.
DR   AGR; SGD:S000000817; -.
DR   SGD; S000000817; FAA2.
DR   VEuPathDB; FungiDB:YER015W; -.
DR   eggNOG; KOG1256; Eukaryota.
DR   GeneTree; ENSGT00960000189179; -.
DR   HOGENOM; CLU_000022_45_4_1; -.
DR   InParanoid; P39518; -.
DR   OMA; IMARTTY; -.
DR   OrthoDB; 443463at2759; -.
DR   BioCyc; MetaCyc:YER015W-MONOMER; -.
DR   BioCyc; YEAST:YER015W-MONOMER; -.
DR   BRENDA; 6.2.1.3; 984.
DR   Reactome; R-SCE-2046105; Linoleic acid (LA) metabolism.
DR   Reactome; R-SCE-2046106; alpha-linolenic acid (ALA) metabolism.
DR   Reactome; R-SCE-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   BioGRID-ORCS; 856734; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P39518; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P39518; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:RHEA.
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:0031957; F:very long-chain fatty acid-CoA ligase activity; IGI:SGD.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IMP:UniProtKB.
DR   GO; GO:0015916; P:fatty-acyl-CoA transport; IGI:UniProtKB.
DR   GO; GO:0015910; P:long-chain fatty acid import into peroxisome; IGI:UniProtKB.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IMP:SGD.
DR   GO; GO:0042760; P:very long-chain fatty acid catabolic process; IGI:UniProtKB.
DR   CDD; cd05927; LC-FACS_euk; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR045311; LC-FACS_euk.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43272:SF3; LONG-CHAIN-FATTY-ACID--COA LIGASE 5; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Magnesium; Membrane; Nucleotide-binding; Peroxisome; Reference proteome.
FT   CHAIN           1..744
FT                   /note="Long-chain-fatty-acid--CoA ligase 2"
FT                   /id="PRO_0000193120"
FT   MOTIF           567..617
FT                   /note="FACS"
FT                   /evidence="ECO:0000250|UniProtKB:P30624"
FT   MOTIF           742..744
FT                   /note="C-terminal peroxisome targeting signal (PTS1)"
FT                   /evidence="ECO:0000305|PubMed:8670886"
FT   BINDING         299..310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69451"
FT   MUTAGEN         1
FT                   /note="M->MWKNAGYKKRIRTNLFRNM: In FAM1-1; extragenic
FT                   suppressor mutation, which creates a new initiation codon
FT                   and adds 18 amino acids to the N-terminus of the protein.
FT                   This extension has all the characteristics of a
FT                   mitochondrial targeting sequence and the FAM1-1 mutant
FT                   protein is indeed imported into the mitochondria, where it
FT                   restores respiratory growth to a deletion of the
FT                   mitochondrial beta-keto-acyl synthase CEM1."
FT                   /evidence="ECO:0000269|PubMed:7988550"
SQ   SEQUENCE   744 AA;  83438 MW;  1E023C18682805BC CRC64;
     MAAPDYALTD LIESDPRFES LKTRLAGYTK GSDEYIEELY SQLPLTSYPR YKTFLKKQAV
     AISNPDNEAG FSSIYRSSLS SENLVSCVDK NLRTAYDHFM FSARRWPQRD CLGSRPIDKA
     TGTWEETFRF ESYSTVSKRC HNIGSGILSL VNTKRKRPLE ANDFVVAILS HNNPEWILTD
     LACQAYSLTN TALYETLGPN TSEYILNLTE APILIFAKSN MYHVLKMVPD MKFVNTLVCM
     DELTHDELRM LNESLLPVKC NSLNEKITFF SLEQVEQVGC FNKIPAIPPT PDSLYTISFT
     SGTTGLPKGV EMSHRNIASG IAFAFSTFRI PPDKRNQQLY DMCFLPLAHI FERMVIAYDL
     AIGFGIGFLH KPDPTVLVED LKILKPYAVA LVPRILTRFE AGIKNALDKS TVQRNVANTI
     LDSKSARFTA RGGPDKSIMN FLVYHRVLID KIRDSLGLSN NSFIITGSAP ISKDTLLFLR
     SALDIGIRQG YGLTETFAGV CLSEPFEKDV GSCGAIGISA ECRLKSVPEM GYHADKDLKG
     ELQIRGPQVF ERYFKNPNET SKAVDQDGWF STGDVAFIDG KGRISVIDRV KNFFKLAHGE
     YIAPEKIENI YLSSCPYITQ IFVFGDPLKT FLVGIVGVDV DAAQPILAAK HPEVKTWTKE
     VLVENLNRNK KLRKEFLNKI NKCTDGLQGF EKLHNIKVGL EPLTLEDDVV TPTFKIKRAK
     ASKFFKDTLD QLYAEGSLVK TEKL
//