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 27-MAR-2024, entry version 128. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q8LKS5; -. DR SwissLipids; SLP:000001940; -. DR PaxDb; 3702-AT5G27600-1; -. 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; AT5G27600; LACS7. DR eggNOG; KOG1256; Eukaryota. DR HOGENOM; CLU_000022_45_4_1; -. DR InParanoid; Q8LKS5; -. DR OMA; IMARTTY; -. DR OrthoDB; 22305at2759; -. DR PhylomeDB; Q8LKS5; -. DR BioCyc; ARA:AT5G27600-MONOMER; -. DR BioCyc; MetaCyc:AT5G27600-MONOMER; -. DR UniPathway; UPA00199; -. DR PRO; PR:Q8LKS5; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q8LKS5; baseline and differential. 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; 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:SF90; LONG CHAIN ACYL-COA SYNTHETASE 7, PEROXISOMAL; 1. DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1. DR Pfam; PF00501; AMP-binding; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. DR Genevisible; Q8LKS5; AT. 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 //