LACS5_ARATH
ID LACS5_ARATH Reviewed; 666 AA.
AC Q9T009; O81614; Q8LKS7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Long chain acyl-CoA synthetase 5;
DE EC=6.2.1.3;
GN Name=LACS5; OrderedLocusNames=At4g11030; ORFNames=F8M12.15, T22B4.10;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAC33962.1; Type=Erroneous gene model prediction; Evidence={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; AF503755; AAM28872.1; -; mRNA.
DR EMBL; AF080118; AAC33962.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL049876; CAB43038.1; -; Genomic_DNA.
DR EMBL; AL161518; CAB81204.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82963.1; -; Genomic_DNA.
DR EMBL; BT046194; ACI49793.1; -; mRNA.
DR PIR; T01875; T01875.
DR PIR; T04298; T04298.
DR PIR; T08182; T08182.
DR RefSeq; NP_192841.1; NM_117173.2.
DR AlphaFoldDB; Q9T009; -.
DR SMR; Q9T009; -.
DR STRING; 3702.AT4G11030.1; -.
DR PaxDb; Q9T009; -.
DR PRIDE; Q9T009; -.
DR ProteomicsDB; 237055; -.
DR EnsemblPlants; AT4G11030.1; AT4G11030.1; AT4G11030.
DR GeneID; 826704; -.
DR Gramene; AT4G11030.1; AT4G11030.1; AT4G11030.
DR KEGG; ath:AT4G11030; -.
DR Araport; AT4G11030; -.
DR TAIR; locus:2136148; AT4G11030.
DR eggNOG; KOG1256; Eukaryota.
DR HOGENOM; CLU_000022_45_4_1; -.
DR InParanoid; Q9T009; -.
DR OMA; CEDPKAK; -.
DR OrthoDB; 630541at2759; -.
DR PhylomeDB; Q9T009; -.
DR BioCyc; ARA:AT4G11030-MON; -.
DR BioCyc; MetaCyc:AT4G11030-MON; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9T009; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T009; baseline and differential.
DR Genevisible; Q9T009; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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..666
FT /note="Long chain acyl-CoA synthetase 5"
FT /id="PRO_0000401413"
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"
FT CONFLICT 661
FT /note="S -> T (in Ref. 1; AAM28872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 74064 MW; 6928569968215C90 CRC64;
MTSQKRFIFE VEAAKEATDG NPSVGPVYRS TFAQNGFPNP IDGIQSCWDI FRTAVEKYPN
NRMLGRREIS NGKAGKYVWK TYKEVYDIVI KLGNSLRSCG IKEGEKCGIY GINCCEWIIS
MEACNAHGLY CVPLYDTLGA GAVEFIISHA EVSIAFVEEK KIPELFKTCP NSTKYMKTVV
SFGGVKPEQK EEAEKLGLVI HSWDEFLKLG EGKQYELPIK KPSDICTIMY TSGTTGDPKG
VMISNESIVT ITTGVMHFLG NVNASLSEKD VYISYLPLAH VFDRAIEECI IQVGGSIGFW
RGDVKLLIED LGELKPSIFC AVPRVLDRVY TGLQQKLSGG GFFKKKVFDV AFSYKFGNMK
KGQSHVAASP FCDKLVFNKV KQGLGGNVRI ILSGAAPLAS HIESFLRVVA CCNVLQGYGL
TESCAGTFAT FPDELDMLGT VGPPVPNVDI RLESVPEMNY DALGSTPRGE ICIRGKTLFS
GYYKREDLTK EVFIDGWLHT GDVGEWQPNG SMKIIDRKKN IFKLAQGEYV AVENLENVYS
QVEVIESIWV YGNSFESFLV AIANPAQQTL ERWAVENGVN GDFNSICQNA KAKAFILGEL
VKTAKENKLK GFEIIKDVHL EPVAFDMERD LLTPTYKKKR PQLLKYYQNV IHEMYKTTKE
SLASGQ
