LACS9_ARATH
ID LACS9_ARATH Reviewed; 691 AA.
AC Q9CAP8; Q0WLQ0; Q84WQ8;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Long chain acyl-CoA synthetase 9, chloroplastic;
DE EC=6.2.1.3;
GN Name=LACS9; OrderedLocusNames=At1g77590; ORFNames=T5M16.18;
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] OF 293-691.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-691.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12177483; DOI=10.1104/pp.003251;
RA Schnurr J.A., Shockey J.M., de Boer G.J., Browse J.A.;
RT "Fatty acid export from the chloroplast. Molecular characterization of a
RT major plastidial acyl-coenzyme A synthetase from Arabidopsis.";
RL Plant Physiol. 129:1700-1709(2002).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS 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 {ECO:0000269|PubMed:12177483}.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast envelope
CC {ECO:0000269|PubMed:12177483}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing seeds and young
CC rosette leaves. {ECO:0000269|PubMed:12177483}.
CC -!- DISRUPTION PHENOTYPE: Reduced amount long-chain fatty acid (LCFA).
CC {ECO:0000269|PubMed:12177483}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF503759; AAM28876.1; -; mRNA.
DR EMBL; AC010704; AAG51668.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35996.1; -; Genomic_DNA.
DR EMBL; BT002872; AAO22689.1; -; mRNA.
DR EMBL; AK230143; BAF01957.1; -; mRNA.
DR PIR; D96805; D96805.
DR RefSeq; NP_177882.1; NM_106407.7.
DR AlphaFoldDB; Q9CAP8; -.
DR SMR; Q9CAP8; -.
DR BioGRID; 29313; 1.
DR STRING; 3702.AT1G77590.1; -.
DR iPTMnet; Q9CAP8; -.
DR PaxDb; Q9CAP8; -.
DR PRIDE; Q9CAP8; -.
DR ProteomicsDB; 237053; -.
DR EnsemblPlants; AT1G77590.1; AT1G77590.1; AT1G77590.
DR GeneID; 844094; -.
DR Gramene; AT1G77590.1; AT1G77590.1; AT1G77590.
DR KEGG; ath:AT1G77590; -.
DR Araport; AT1G77590; -.
DR TAIR; locus:2204765; AT1G77590.
DR eggNOG; KOG1180; Eukaryota.
DR HOGENOM; CLU_000022_45_2_1; -.
DR InParanoid; Q9CAP8; -.
DR OMA; EWIVRDS; -.
DR OrthoDB; 293865at2759; -.
DR PhylomeDB; Q9CAP8; -.
DR BioCyc; ARA:AT1G77590-MON; -.
DR BioCyc; MetaCyc:AT1G77590-MON; -.
DR SABIO-RK; Q9CAP8; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9CAP8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAP8; baseline and differential.
DR Genevisible; Q9CAP8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:TAIR.
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 ATP-binding; Chloroplast; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Magnesium; Nucleotide-binding; Plastid; Reference proteome.
FT CHAIN 1..691
FT /note="Long chain acyl-CoA synthetase 9, chloroplastic"
FT /id="PRO_0000401418"
FT REGION 525..553
FT /note="Fatty acid-binding"
FT /evidence="ECO:0000255"
FT BINDING 250..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 293
FT /note="Y -> F (in Ref. 4; AAO22689)"
FT /evidence="ECO:0000305"
FT CONFLICT 586..587
FT /note="AD -> SS (in Ref. 5; BAF01957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 76176 MW; 8B01B936CF91F564 CRC64;
MIPYAAGVIV PLALTFLVQK SKKEKKRGVV VDVGGEPGYA IRNHRFTEPV SSHWEHISTL
PELFEISCNA HSDRVFLGTR KLISREIETS EDGKTFEKLH LGDYEWLTFG KTLEAVCDFA
SGLVQIGHKT EERVAIFADT REEWFISLQG CFRRNVTVVT IYSSLGEEAL CHSLNETEVT
TVICGSKELK KLMDISQQLE TVKRVICMDD EFPSDVNSNW MATSFTDVQK LGRENPVDPN
FPLSADVAVI MYTSGSTGLP KGVMMTHGNV LATVSAVMTI VPDLGKRDIY MAYLPLAHIL
ELAAESVMAT IGSAIGYGSP LTLTDTSNKI KKGTKGDVTA LKPTIMTAVP AILDRVRDGV
RKKVDAKGGL SKKLFDFAYA RRLSAINGSW FGAWGLEKLL WDVLVFRKIR AVLGGQIRYL
LSGGAPLSGD TQRFINICVG APIGQGYGLT ETCAGGTFSE FEDTSVGRVG APLPCSFVKL
VDWAEGGYLT SDKPMPRGEI VIGGSNITLG YFKNEEKTKE VYKVDEKGMR WFYTGDIGRF
HPDGCLEIID RKKDIVKLQH GEYVSLGKVE AALSISPYVE NIMVHADSFY SYCVALVVAS
QHTVEGWASK QGIDFANFEE LCTKEQAVKE VYASLVKAAK QSRLEKFEIP AKIKLLASPW
TPESGLVTAA LKLKRDVIRR EFSEDLTKLY A
