LACS7_ARATH
ID LACS7_ARATH Reviewed; 700 AA.
AC Q8LKS5; Q8GWV4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Long chain acyl-CoA synthetase 7, peroxisomal {ECO:0000303|PubMed:12177484};
DE Short=AtLACS7 {ECO:0000303|PubMed:12366803};
DE EC=6.2.1.3 {ECO:0000269|PubMed:12177484, ECO:0000269|PubMed:12366803};
GN Name=LACS7 {ECO:0000303|PubMed:12177484};
GN OrderedLocusNames=At5g27600 {ECO:0000312|EMBL:AED93704.1};
GN ORFNames=F15A18.60 {ECO:0000312|EMBL:AC007478};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-700.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
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 [6]
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 [7]
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 [8]
RP INTERACTION WITH PEX5, 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 [9]
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
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). Functions
CC redundantly with LACS6 in lipid mobilization for beta-oxidation during
CC seed germination, which is essential for postgerminative growth and
CC seedling establishment (PubMed:14742880, PubMed:16844736).
CC {ECO:0000269|PubMed:12177484, ECO:0000269|PubMed:12366803,
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 + 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:12366803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000269|PubMed:12366803};
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:12366803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={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 -!- SUBUNIT: Interacts with PEX5. {ECO:0000269|PubMed:16256065}.
CC -!- INTERACTION:
CC Q8LKS5; Q9FMA3: PEX5; NbExp=4; IntAct=EBI-993851, EBI-993861;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12366803}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves flowers and
CC germinating seedling (PubMed:12177484). Preferentially expressed in
CC seeds. {ECO:0000269|PubMed:12177484, ECO:0000269|PubMed:16256065}.
CC -!- DEVELOPMENTAL STAGE: Induced during seed germination.
CC {ECO:0000269|PubMed:12366803}.
CC -!- INDUCTION: Up-regulated by ozone and salt stress.
CC {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=BAC43213.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF503757; AAM28874.1; -; mRNA.
DR EMBL; AC007478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93704.1; -; Genomic_DNA.
DR EMBL; AK118614; BAC43213.1; ALT_INIT; mRNA.
DR RefSeq; NP_198112.2; NM_122642.5.
DR AlphaFoldDB; Q8LKS5; -.
DR SMR; Q8LKS5; -.
DR BioGRID; 18094; 2.
DR IntAct; Q8LKS5; 1.
DR STRING; 3702.AT5G27600.1; -.
DR SwissLipids; SLP:000001940; -.
DR PaxDb; Q8LKS5; -.
DR PRIDE; Q8LKS5; -.
DR ProteomicsDB; 237056; -.
DR EnsemblPlants; AT5G27600.1; AT5G27600.1; AT5G27600.
DR GeneID; 832820; -.
DR Gramene; AT5G27600.1; AT5G27600.1; AT5G27600.
DR KEGG; ath:AT5G27600; -.
DR Araport; AT5G27600; -.
DR TAIR; locus:2143661; AT5G27600.
DR eggNOG; KOG1256; Eukaryota.
DR HOGENOM; CLU_000022_45_4_1; -.
DR InParanoid; Q8LKS5; -.
DR OMA; NRGELCV; -.
DR OrthoDB; 630541at2759; -.
DR PhylomeDB; Q8LKS5; -.
DR BioCyc; ARA:AT5G27600-MON; -.
DR BioCyc; MetaCyc:AT5G27600-MON; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q8LKS5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LKS5; baseline and differential.
DR Genevisible; Q8LKS5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:UniProtKB.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
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; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium;
KW Nucleotide-binding; Peroxisome; Reference proteome.
FT CHAIN 1..700
FT /note="Long chain acyl-CoA synthetase 7, peroxisomal"
FT /id="PRO_0000401416"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..550
FT /note="Fatty acid-binding"
FT /evidence="ECO:0000255"
FT MOTIF 10..18
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOTIF 698..700
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 266..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 657
FT /note="F -> L (in Ref. 1; AAM28874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 77353 MW; EAD95B9F50DA75DB CRC64;
MEFASPEQRR LETIRSHIDT SPTNDQSSSL FLNATASSAS PFFKEDSYSV VLPEKLDTGK
WNVYRSKRSP TKLVSRFPDH PEIGTLHDNF VHAVETYAEN KYLGTRVRSD GTIGEYSWMT
YGEAASERQA IGSGLLFHGV NQGDCVGLYF INRPEWLVVD HACAAYSFVS VPLYDTLGPD
AVKFVVNHAN LQAIFCVPQT LNILLSFLAE IPSIRLIVVV GGADEHLPSL PRGTGVTIVS
YQKLLSQGRS SLHPFSPPKP EDIATICYTS GTTGTPKGVV LTHGNLIANV AGSSVEAEFF
PSDVYISYLP LAHIYERANQ IMGVYGGVAV GFYQGDVFKL MDDFAVLRPT IFCSVPRLYN
RIYDGITSAV KSSGVVKKRL FEIAYNSKKQ AIINGRTPSA FWDKLVFNKI KEKLGGRVRF
MGSGASPLSP DVMDFLRICF GCSVREGYGM TETSCVISAM DDGDNLSGHV GSPNPACEVK
LVDVPEMNYT SDDQPYPRGE ICVRGPIIFK GYYKDEEQTR EILDGDGWLH TGDIGLWLPG
GRLKIIDRKK NIFKLAQGEY IAPEKIENVY TKCRFVSQCF IHGDSFNSSL VAIVSVDPEV
MKDWAASEGI KYEHLGQLCN DPRVRKTVLA EMDDLGREAQ LRGFEFAKAV TLVPEPFTLE
NGLLTPTFKI KRPQAKAYFA EAISKMYAEI AASNPIPSKL
