ID   LACS8_ARATH             Reviewed;         720 AA.
AC   Q9SJD4; Q940V0;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Long chain acyl-CoA synthetase 8;
DE            EC=6.2.1.3;
GN   Name=LACS8; OrderedLocusNames=At2g04350; ORFNames=T1O3, T23O15.3;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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; AF503758; AAM28875.1; -; mRNA.
DR   EMBL; AC006951; AAD25843.1; -; Genomic_DNA.
DR   EMBL; AC007213; AAM15458.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05822.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05823.1; -; Genomic_DNA.
DR   EMBL; AY052664; AAK96568.1; -; mRNA.
DR   EMBL; BT002288; AAN72299.1; -; mRNA.
DR   PIR; E84456; E84456.
DR   RefSeq; NP_178516.1; NM_126468.4.
DR   RefSeq; NP_849934.1; NM_179603.2.
DR   AlphaFoldDB; Q9SJD4; -.
DR   SMR; Q9SJD4; -.
DR   BioGRID; 375; 4.
DR   STRING; 3702.Q9SJD4; -.
DR   iPTMnet; Q9SJD4; -.
DR   PaxDb; 3702-AT2G04350-1; -.
DR   ProteomicsDB; 237119; -.
DR   EnsemblPlants; AT2G04350.1; AT2G04350.1; AT2G04350.
DR   EnsemblPlants; AT2G04350.2; AT2G04350.2; AT2G04350.
DR   GeneID; 814974; -.
DR   Gramene; AT2G04350.1; AT2G04350.1; AT2G04350.
DR   Gramene; AT2G04350.2; AT2G04350.2; AT2G04350.
DR   KEGG; ath:AT2G04350; -.
DR   Araport; AT2G04350; -.
DR   TAIR; AT2G04350; LACS8.
DR   eggNOG; KOG1180; Eukaryota.
DR   HOGENOM; CLU_000022_45_2_1; -.
DR   InParanoid; Q9SJD4; -.
DR   OMA; KIFQWAA; -.
DR   OrthoDB; 443463at2759; -.
DR   PhylomeDB; Q9SJD4; -.
DR   BioCyc; ARA:AT2G04350-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G04350-MONOMER; -.
DR   SABIO-RK; Q9SJD4; -.
DR   UniPathway; UPA00199; -.
DR   PRO; PR:Q9SJD4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJD4; baseline and differential.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; 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; cd17639; LC_FACS_euk1; 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   PANTHER; PTHR43272:SF92; LONG CHAIN ACYL-COA SYNTHETASE 8; 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; Q9SJD4; AT.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Magnesium; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..720
FT                   /note="Long chain acyl-CoA synthetase 8"
FT                   /id="PRO_0000401417"
FT   REGION          554..582
FT                   /note="Fatty acid-binding"
FT                   /evidence="ECO:0000255"
FT   BINDING         279..290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CONFLICT        256..263
FT                   /note="EVEKLGQK -> DFFKLPPH (in Ref. 4; AAK96568)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   720 AA;  78343 MW;  96ED3FD23AD2ED75 CRC64;
     MEDSGVNPMD SPSKGSDFGV YGIIGGGIVA LLVPVLLSVV LNGTKKGKKR GVPIKVGGEE
     GYTMRHARAP ELVDVPWEGA ATMPALFEQS CKKYSKDRLL GTREFIDKEF ITASDGRKFE
     KLHLGEYKWQ SYGEVFERVC NFASGLVNVG HNVDDRVAIF SDTRAEWFIA FQGCFRQSIT
     VVTIYASLGE EALIYSLNET RVSTLICDSK QLKKLSAIQS SLKTVKNIIY IEEDGVDVAS
     SDVNSMGDIT VSSISEVEKL GQKNAVQPIL PSKNGVAVIM FTSGSTGLPK GVMITHGNLV
     ATAAGVMKVV PKLDKNDTYI AYLPLAHVFE LEAEIVVFTS GSAIGYGSAM TLTDTSNKVK
     KGTKGDVSAL KPTIMTAVPA ILDRVREGVL KKVEEKGGMA KTLFDFAYKR RLAAVDGSWF
     GAWGLEKMLW DALVFKKIRA VLGGHIRFML VGGAPLSPDS QRFINICMGS PIGQGYGLTE
     TCAGATFSEW DDPAVGRVGP PLPCGYVKLV SWEEGGYRIS DKPMPRGEIV VGGNSVTAGY
     FNNQEKTDEV YKVDEKGTRW FYTGDIGRFH PDGCLEVIDR KKDIVKLQHG EYVSLGKVEA
     ALGSSNYVDN IMVHADPINS YCVALVVPSR GALEKWAEEA GVKHSEFAEL CEKGEAVKEV
     QQSLTKAGKA AKLEKFELPA KIKLLSEPWT PESGLVTAAL KIKREQIKSK FKDELSKLYA
//