ID LACS3_ARATH Reviewed; 665 AA. AC Q9C7W4; DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=Long chain acyl-CoA synthetase 3; DE EC=6.2.1.3; GN Name=LACS3; OrderedLocusNames=At1g64400; ORFNames=F15H21.7; 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], GENE FAMILY, AND ENZYME ACTIVITY. 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=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(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]. 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 [5] 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). CC -!- FUNCTION: Activation of long-chain fatty acids for both synthesis of CC cellular lipids, and degradation via beta-oxidation. Preferentially CC uses palmitate, palmitoleate, oleate and linoleate. 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}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC {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; AF503753; AAM28870.1; -; mRNA. DR EMBL; AC066689; AAG51719.1; -; Genomic_DNA. DR EMBL; CP002684; AEE34237.1; -; Genomic_DNA. DR EMBL; AY039935; AAK64039.1; -; mRNA. DR EMBL; AY079314; AAL85045.1; -; mRNA. DR PIR; B96668; B96668. DR RefSeq; NP_176622.1; NM_105115.4. DR AlphaFoldDB; Q9C7W4; -. DR SMR; Q9C7W4; -. DR STRING; 3702.Q9C7W4; -. DR iPTMnet; Q9C7W4; -. DR PaxDb; 3702-AT1G64400-1; -. DR ProteomicsDB; 238653; -. DR EnsemblPlants; AT1G64400.1; AT1G64400.1; AT1G64400. DR GeneID; 842748; -. DR Gramene; AT1G64400.1; AT1G64400.1; AT1G64400. DR KEGG; ath:AT1G64400; -. DR Araport; AT1G64400; -. DR TAIR; AT1G64400; LACS3. DR eggNOG; KOG1256; Eukaryota. DR HOGENOM; CLU_000022_45_4_1; -. DR InParanoid; Q9C7W4; -. DR OMA; HGLTIYS; -. DR OrthoDB; 22305at2759; -. DR PhylomeDB; Q9C7W4; -. DR BioCyc; ARA:AT1G64400-MONOMER; -. DR BioCyc; MetaCyc:AT1G64400-MONOMER; -. DR UniPathway; UPA00199; -. DR PRO; PR:Q9C7W4; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9C7W4; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR. 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 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:SF42; LONG CHAIN ACYL-COA SYNTHETASE 3; 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; Q9C7W4; AT. PE 2: Evidence at transcript level; KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..665 FT /note="Long chain acyl-CoA synthetase 3" FT /id="PRO_0000401411" FT REGION 495..519 FT /note="Fatty acid-binding" FT /evidence="ECO:0000255" FT BINDING 228..239 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" SQ SEQUENCE 665 AA; 74751 MW; B546A845F101DB6C CRC64; MATGRYIVEV EKGKQGVDGG SPSVGPVYRS IYAKDGFPEP PDDLVSAWDI FRLSVEKSPN NPMLGRREIV DGKAGKYVWQ TYKEVHNVVI KLGNSIRTIG VGKGDKCGIY GANSPEWIIS MEACNAHGLY CVPLYDTLGA GAIEFIICHA EVSLAFAEEN KISELLKTAP KSTKYLKYIV SFGEVTNNQR VEAERHRLTI YSWDQFLKLG EGKHYELPEK RRSDVCTIMY TSGTTGDPKG VLLTNESIIH LLEGVKKLLK TIDEELTSKD VYLSYLPLAH IFDRVIEELC IYEAASIGFW RGDVKILIED IAALKPTVFC AVPRVLERIY TGLQQKLSDG GFVKKKLFNF AFKYKHKNME KGQPHEQASP IADKIVFKKV KEGLGGNVRL ILSGAAPLAA HIESFLRVVA CAHVLQGYGL TESCGGTFVS IPNELSMLGT VGPPVPNVDI RLESVPEMGY DALASNPRGE ICIRGKTLFS GYYKREDLTQ EVFIDGWLHT GDVGEWQPDG AMKIIDRKKN IFKLSQGEYV AVENLENIYS HVAAIESIWV YGNSYESYLV AVVCPSKIQI EHWAKEHKVS GDFESICRNQ KTKEFVLGEF NRVAKDKKLK GFELIKGVHL DTVPFDMERD LITPSYKMKR PQLLKYYQKE IDEMYKKNRE VQLRV //