LACS6_ARATH
ID LACS6_ARATH Reviewed; 701 AA.
AC Q8LPS1; Q8LKS6; Q9C5U7; Q9SFG1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Long chain acyl-CoA synthetase 6, peroxisomal {ECO:0000303|PubMed:12177484};
DE Short=AtLACS6 {ECO:0000303|PubMed:12366803};
DE EC=6.2.1.3 {ECO:0000269|PubMed:12177484, ECO:0000269|PubMed:12366803};
DE Flags: Precursor;
GN Name=LACS6 {ECO:0000303|PubMed:12177484};
GN OrderedLocusNames=At3g05970 {ECO:0000312|EMBL:AEE74324.1};
GN ORFNames=F2O10.7 {ECO:0000312|EMBL:AAF23219.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND GENE FAMILY.
RX PubMed=12177484; DOI=10.1104/pp.003269;
RA Shockey J.M., Fulda M.S., Browse J.A.;
RT "Arabidopsis contains nine long-chain acyl-coenzyme A synthetase genes that
RT participate in fatty acid and glycerolipid metabolism.";
RL Plant Physiol. 129:1710-1722(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-60, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12481085; DOI=10.1104/pp.012955;
RA Hayashi H., De Bellis L., Hayashi Y., Nito K., Kato A., Hayashi M.,
RA Hara-Nishimura I., Nishimura M.;
RT "Molecular characterization of an Arabidopsis acyl-coenzyme A synthetase
RT localized on glyoxysomal membranes.";
RL Plant Physiol. 130:2019-2026(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12366803; DOI=10.1046/j.1365-313x.2002.01405.x;
RA Fulda M., Shockey J., Werber M., Wolter F.P., Heinz E.;
RT "Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in
RT peroxisomal fatty acid beta-oxidation.";
RL Plant J. 32:93-103(2002).
RN [7]
RP GENE FAMILY ORGANIZATION.
RX PubMed=12805634; DOI=10.1104/pp.103.020552;
RA Shockey J.M., Fulda M.S., Browse J.;
RT "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT a synthetases.";
RL Plant Physiol. 132:1065-1076(2003).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14742880; DOI=10.1105/tpc.019646;
RA Fulda M., Schnurr J., Abbadi A., Heinz E., Browse J.;
RT "Peroxisomal Acyl-CoA synthetase activity is essential for seedling
RT development in Arabidopsis thaliana.";
RL Plant Cell 16:394-405(2004).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16256065; DOI=10.1016/j.abb.2005.09.003;
RA Bonsegna S., Slocombe S.P., De Bellis L., Baker A.;
RT "AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5.";
RL Arch. Biochem. Biophys. 443:74-81(2005).
RN [10]
RP FUNCTION.
RX PubMed=16844736; DOI=10.1093/jxb/erl045;
RA Footitt S., Marquez J., Schmuths H., Baker A., Theodoulou F.L.,
RA Holdsworth M.;
RT "Analysis of the role of COMATOSE and peroxisomal beta-oxidation in the
RT determination of germination potential in Arabidopsis.";
RL J. Exp. Bot. 57:2805-2814(2006).
CC -!- FUNCTION: Activation of long-chain fatty acids for both synthesis of
CC cellular lipids, and degradation via beta-oxidation (Probable).
CC Preferentially uses palmitate, palmitoleate, oleate, linoleate and
CC eicosenoate as substrates (PubMed:12177484, PubMed:12366803). Can use
CC myristate and linolenate as substrates (PubMed:12366803). May play a
CC regulatory role both in fatty acid import into glyoxysomes and in fatty
CC acid beta-oxidation (PubMed:12481085). Functions redundantly with LACS7
CC in lipid mobilization for beta-oxidation during seed germination, which
CC is essential for postgerminative growth and seedling establishment
CC (PubMed:14742880, PubMed:16844736). {ECO:0000269|PubMed:12177484,
CC ECO:0000269|PubMed:12366803, ECO:0000269|PubMed:12481085,
CC ECO:0000269|PubMed:14742880, ECO:0000269|PubMed:16844736,
CC ECO:0000305|PubMed:12177484, ECO:0000305|PubMed:12366803}.
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:12177484, ECO:0000269|PubMed:12366803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000269|PubMed:12177484, ECO:0000269|PubMed:12366803};
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:12366803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000269|PubMed:12366803};
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:12366803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000269|PubMed:12366803};
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:12366803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000269|PubMed:12366803};
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:12366803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC Evidence={ECO:0000269|PubMed:12366803};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-
CC octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:12366803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937;
CC Evidence={ECO:0000269|PubMed:12366803};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P69451};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12366803,
CC ECO:0000269|PubMed:12481085}. Glyoxysome membrane
CC {ECO:0000269|PubMed:12481085}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves flowers and
CC germinating seedling (PubMed:12177484). Preferentially expressed in
CC seeds and senescent leaves. {ECO:0000269|PubMed:12177484,
CC ECO:0000269|PubMed:16256065}.
CC -!- DEVELOPMENTAL STAGE: Induced during seed germination.
CC {ECO:0000269|PubMed:12366803}.
CC -!- INDUCTION: Up-regulated by ozone. {ECO:0000269|PubMed:16256065}.
CC -!- DISRUPTION PHENOTYPE: Seedlings of the lacs6 and lacs7 double mutant
CC were arrested in postgerminative growth due to inability to mobilize
CC fatty acids for beta-oxidation, a necessary process to pursue the
CC development. {ECO:0000269|PubMed:14742880}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23219.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF503756; AAM28873.1; -; mRNA.
DR EMBL; AB030317; BAB40450.1; -; mRNA.
DR EMBL; AC013454; AAF23219.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74324.1; -; Genomic_DNA.
DR EMBL; AY094418; AAM19792.1; -; mRNA.
DR EMBL; BT001117; AAN64508.1; -; mRNA.
DR RefSeq; NP_566265.1; NM_111471.3.
DR AlphaFoldDB; Q8LPS1; -.
DR SMR; Q8LPS1; -.
DR BioGRID; 5102; 2.
DR STRING; 3702.AT3G05970.1; -.
DR SwissLipids; SLP:000001941; -.
DR PaxDb; Q8LPS1; -.
DR PRIDE; Q8LPS1; -.
DR ProteomicsDB; 238554; -.
DR EnsemblPlants; AT3G05970.1; AT3G05970.1; AT3G05970.
DR GeneID; 819767; -.
DR Gramene; AT3G05970.1; AT3G05970.1; AT3G05970.
DR KEGG; ath:AT3G05970; -.
DR Araport; AT3G05970; -.
DR TAIR; locus:2083013; AT3G05970.
DR eggNOG; KOG1256; Eukaryota.
DR HOGENOM; CLU_000022_45_4_1; -.
DR InParanoid; Q8LPS1; -.
DR OMA; PRIWTKF; -.
DR OrthoDB; 630541at2759; -.
DR PhylomeDB; Q8LPS1; -.
DR BioCyc; ARA:AT3G05970-MON; -.
DR BioCyc; MetaCyc:AT3G05970-MON; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q8LPS1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LPS1; baseline and differential.
DR Genevisible; Q8LPS1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0046861; C:glyoxysomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:UniProtKB.
DR GO; GO:0010193; P:response to ozone; IEP:UniProtKB.
DR CDD; cd05927; LC-FACS_euk; 1.
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 InterPro; IPR045311; LC-FACS_euk.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Direct protein sequencing;
KW Fatty acid metabolism; Glyoxysome; Ligase; Lipid metabolism; Magnesium;
KW Membrane; Nucleotide-binding; Peroxisome; Reference proteome.
FT PROPEP 1..38
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:12481085"
FT /id="PRO_0000401414"
FT CHAIN 39..701
FT /note="Long chain acyl-CoA synthetase 6, peroxisomal"
FT /id="PRO_0000401415"
FT REGION 526..550
FT /note="Fatty acid-binding"
FT /evidence="ECO:0000255"
FT MOTIF 15..23
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305|PubMed:12481085"
FT BINDING 266..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 60
FT /note="S -> N (in Ref. 2; BAB40450)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="G -> V (in Ref. 1; AAM28873)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="I -> N (in Ref. 2; BAB40450)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="V -> I (in Ref. 1; AAM28873)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="I -> V (in Ref. 2; BAB40450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 76603 MW; 4A0F06A05FA13022 CRC64;
MDSSSSSSSA AARRRINAIH SHLVTSSRSS PLLRSNPTAG EFCLDNGYSV VLPEKLNTGS
WNVYRSAKSP FKLVSRFPDH PDIATLHDNF EHAVHDFRDY KYLGTRVRVD GTVGDYKWMT
YGEAGTARTA LGSGLVHHGI PMGSSVGIYF INRPEWLIVD HACSSYSYVS VPLYDTLGPD
AVKFIVNHAT VQAIFCVAET LNSLLSCLSE MPSVRLVVVV GGLIESLPSL PSSSGVKVVS
YSVLLNQGRS NPQRFFPPKP DDVATICYTS GTTGTPKGVV LTHANLIANV AGSSFSVKFF
SSDVYISYLP LAHIYERANQ ILTVYFGVAV GFYQGDNMKL LDDLAALRPT VFSSVPRLYN
RIYAGIINAV KTSGGLKERL FNAAYNAKKQ ALLNGKSASP IWDRLVFNKI KDRLGGRVRF
MTSGASPLSP EVMEFLKVCF GGRVTEGYGM TETSCVISGM DEGDNLTGHV GSPNPACEVK
LVDVPEMNYT SADQPHPRGE ICVRGPIIFT GYYKDEIQTK EVIDEDGWLH TGDIGLWLPG
GRLKIIDRKK NIFKLAQGEY IAPEKIENVY AKCKFVGQCF IYGDSFNSSL VAVVSVDPDV
LKSWAASEGI KGGDLRELCN NPRVKAAVLS DMDTVGREAQ LRGFEFAKAV TLVLEPFTLE
NGLLTPTFKI KRPQAKEYFA EAITNMYKEL GASDPSANRG L
