ACS_ARATH
ID ACS_ARATH Reviewed; 743 AA.
AC B9DGD6; O49063; Q9LTG4;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Acetyl-coenzyme A synthetase, chloroplastic/glyoxysomal;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase;
DE AltName: Full=Acetyl-CoA synthetase;
DE Flags: Precursor;
GN Name=ACS; OrderedLocusNames=At5g36880; ORFNames=F5H8.15;
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] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10859180; DOI=10.1104/pp.123.2.497;
RA Ke J., Behal R.H., Back S.L., Nikolau B.J., Wurtele E.S., Oliver D.J.;
RT "The role of pyruvate dehydrogenase and acetyl-coenzyme A synthetase in
RT fatty acid synthesis in developing Arabidopsis seeds.";
RL Plant Physiol. 123:497-508(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 2).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION.
RX PubMed=12051672; DOI=10.1016/s0003-9861(02)00086-3;
RA Behal R.H., Lin M., Back S., Oliver D.J.;
RT "Role of acetyl-coenzyme A synthetase in leaves of Arabidopsis thaliana.";
RL Arch. Biochem. Biophys. 402:259-267(2002).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=14581625; DOI=10.1093/pcp/pcg145;
RA Fukao Y., Hayashi M., Hara-Nishimura I., Nishimura M.;
RT "Novel glyoxysomal protein kinase, GPK1, identified by proteomic analysis
RT of glyoxysomes in etiolated cotyledons of Arabidopsis thaliana.";
RL Plant Cell Physiol. 44:1002-1012(2003).
RN [8]
RP GENE FAMILY.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Catalyzes the production of acetyl-CoA, an activated form of
CC acetate that can be used for lipid synthesis or for energy generation.
CC May play a limited role in the biosynthesis of lipids.
CC {ECO:0000269|PubMed:10859180, ECO:0000269|PubMed:12051672}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC Evidence={ECO:0000269|PubMed:10859180};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Glyoxysome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B9DGD6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DGD6-2; Sequence=VSP_042326;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flower buds and young flowers.
CC {ECO:0000269|PubMed:10859180}.
CC -!- DEVELOPMENTAL STAGE: In the forming silique, expressed in the funiculus
CC and ovule from 1 to 3 day after flowering (DAF). At 3 DAF, expressed in
CC the globular embryo, but expression decreases at 5 DAF and almost
CC disappears at 7 DAF in the embryo. By 1 d after imbibition, expressed
CC in the tip of seed radicle and then in the root tip up to 4 d after
CC imbibition. {ECO:0000269|PubMed:10859180}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF036618; AAB92552.1; -; mRNA.
DR EMBL; AB025605; BAA98066.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94120.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94121.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69414.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69415.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69417.1; -; Genomic_DNA.
DR EMBL; AY045880; AAK76554.1; -; mRNA.
DR EMBL; BT002371; AAN86204.1; -; mRNA.
DR EMBL; AK317115; BAH19803.1; -; mRNA.
DR RefSeq; NP_001031974.2; NM_001036897.3. [B9DGD6-1]
DR RefSeq; NP_001331094.1; NM_001344154.1. [B9DGD6-2]
DR RefSeq; NP_001331095.1; NM_001344156.1. [B9DGD6-2]
DR RefSeq; NP_001331097.1; NM_001344157.1. [B9DGD6-2]
DR RefSeq; NP_198504.1; NM_123046.4. [B9DGD6-2]
DR AlphaFoldDB; B9DGD6; -.
DR SMR; B9DGD6; -.
DR BioGRID; 18906; 4.
DR STRING; 3702.AT5G36880.2; -.
DR iPTMnet; B9DGD6; -.
DR MetOSite; B9DGD6; -.
DR PaxDb; B9DGD6; -.
DR PRIDE; B9DGD6; -.
DR ProteomicsDB; 244386; -. [B9DGD6-1]
DR EnsemblPlants; AT5G36880.1; AT5G36880.1; AT5G36880. [B9DGD6-2]
DR EnsemblPlants; AT5G36880.2; AT5G36880.2; AT5G36880. [B9DGD6-1]
DR EnsemblPlants; AT5G36880.3; AT5G36880.3; AT5G36880. [B9DGD6-2]
DR EnsemblPlants; AT5G36880.5; AT5G36880.5; AT5G36880. [B9DGD6-2]
DR EnsemblPlants; AT5G36880.6; AT5G36880.6; AT5G36880. [B9DGD6-2]
DR GeneID; 833655; -.
DR Gramene; AT5G36880.1; AT5G36880.1; AT5G36880. [B9DGD6-2]
DR Gramene; AT5G36880.2; AT5G36880.2; AT5G36880. [B9DGD6-1]
DR Gramene; AT5G36880.3; AT5G36880.3; AT5G36880. [B9DGD6-2]
DR Gramene; AT5G36880.5; AT5G36880.5; AT5G36880. [B9DGD6-2]
DR Gramene; AT5G36880.6; AT5G36880.6; AT5G36880. [B9DGD6-2]
DR KEGG; ath:AT5G36880; -.
DR Araport; AT5G36880; -.
DR TAIR; locus:2149104; AT5G36880.
DR eggNOG; KOG1175; Eukaryota.
DR InParanoid; B9DGD6; -.
DR OMA; DHWWHDL; -.
DR OrthoDB; 288915at2759; -.
DR PhylomeDB; B9DGD6; -.
DR BioCyc; ARA:AT5G36880-MON; -.
DR BRENDA; 6.2.1.1; 399.
DR PRO; PR:B9DGD6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B9DGD6; baseline and differential.
DR Genevisible; B9DGD6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IMP:TAIR.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006083; P:acetate metabolic process; IMP:TAIR.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chloroplast; Fatty acid metabolism;
KW Glyoxysome; Ligase; Lipid metabolism; Nucleotide-binding; Peroxisome;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..84
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 85..743
FT /note="Acetyl-coenzyme A synthetase,
FT chloroplastic/glyoxysomal"
FT /id="PRO_0000415733"
FT ACT_SITE 613
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10859180,
FT ECO:0000303|PubMed:14593172"
FT /id="VSP_042326"
FT CONFLICT 426
FT /note="F -> L (in Ref. 1; AAB92552)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="W -> R (in Ref. 1; AAB92552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 743 AA; 81889 MW; 774E5ACE90046A0E CRC64;
MKIGSPSSPI LSVVSSSGSL DPKISGSLGS RILPATQRSS PSENLLLHRK MSSNSLRHVE
SMSQLPSGAG KISQLNAVVL GESLASEEND LVFPSKEFSG QALVSSPQQY MEMHKRSMDD
PAAFWSDIAS EFYWKQKWGD QVFSENLDVR KGPISIEWFK GGITNICYNC LDKNVEAGLG
DKTAIHWEGN ELGVDASLTY SELLQRVCQL ANYLKDNGVK KGDAVVIYLP MLMELPIAML
ACARIGAVHS VVFAGFSADS LAQRIVDCKP NVILTCNAVK RGPKTINLKA IVDAALDQSS
KDGVSVGICL TYDNSLATTR ENTKWQNGRD VWWQDVISQY PTSCEVEWVD AEDPLFLLYT
SGSTGKPKGV LHTTGGYMIY TATTFKYAFD YKSTDVYWCT ADCGWITGHS YVTYGPMLNG
ATVVVFEGAP NYPDPGRCWD IVDKYKVSIF YTAPTLVRSL MRDDDKFVTR HSRKSLRVLG
SVGEPINPSA WRWFFNVVGD SRCPISDTWW QTETGGFMIT PLPGAWPQKP GSATFPFFGV
QPVIVDEKGN EIEGECSGYL CVKGSWPGAF RTLFGDHERY ETTYFKPFAG YYFSGDGCSR
DKDGYYWLTG RVDDVINVSG HRIGTAEVES ALVLHPQCAE AAVVGIEHEV KGQGIYAFVT
LLEGVPYSEE LRKSLVLMVR NQIGAFAAPD RIHWAPGLPK TRSGKIMRRI LRKIASRQLE
ELGDTSTLAD PSVVDQLIAL ADV
