LACS8_ARATH
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 03-AUG-2022, entry version 135.
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.AT2G04350.1; -.
DR iPTMnet; Q9SJD4; -.
DR PaxDb; Q9SJD4; -.
DR PRIDE; Q9SJD4; -.
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; locus:2058384; AT2G04350.
DR eggNOG; KOG1180; Eukaryota.
DR HOGENOM; CLU_000022_45_2_1; -.
DR InParanoid; Q9SJD4; -.
DR OMA; KIFQWAA; -.
DR OrthoDB; 293865at2759; -.
DR PhylomeDB; Q9SJD4; -.
DR BioCyc; ARA:AT2G04350-MON; -.
DR BioCyc; MetaCyc:AT2G04350-MON; -.
DR SABIO-RK; Q9SJD4; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9SJD4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJD4; baseline and differential.
DR Genevisible; Q9SJD4; AT.
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:0016020; C:membrane; IBA:GO_Central.
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 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 Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
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