LACS3_ARATH
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 03-AUG-2022, entry version 124.
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}.
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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.AT1G64400.1; -.
DR iPTMnet; Q9C7W4; -.
DR PaxDb; Q9C7W4; -.
DR PRIDE; Q9C7W4; -.
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; locus:2014265; AT1G64400.
DR eggNOG; KOG1256; Eukaryota.
DR HOGENOM; CLU_000022_45_4_1; -.
DR InParanoid; Q9C7W4; -.
DR OMA; RSDVCTI; -.
DR OrthoDB; 630541at2759; -.
DR PhylomeDB; Q9C7W4; -.
DR BioCyc; ARA:AT1G64400-MON; -.
DR BioCyc; MetaCyc:AT1G64400-MON; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9C7W4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7W4; baseline and differential.
DR Genevisible; Q9C7W4; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; -; 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 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
