ACLA1_ARATH
ID ACLA1_ARATH Reviewed; 423 AA.
AC Q9SGY2; Q56WG2; Q8LAY1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ATP-citrate synthase alpha chain protein 1;
DE Short=ATP-citrate synthase A-1;
DE EC=2.3.3.8;
DE AltName: Full=ATP-citrate lyase A-1;
DE AltName: Full=Citrate cleavage enzyme A-1;
GN Name=ACLA-1; OrderedLocusNames=At1g10670; ORFNames=F20B24.11;
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], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=12376641; DOI=10.1104/pp.008110;
RA Fatland B.L., Ke J., Anderson M.D., Mentzen W.I., Cui L.W., Allred C.C.,
RA Johnston J.L., Nikolau B.J., Wurtele E.S.;
RT "Molecular characterization of a heteromeric ATP-citrate lyase that
RT generates cytosolic acetyl-coenzyme A in Arabidopsis.";
RL Plant Physiol. 130:740-756(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].
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=15608338; DOI=10.1105/tpc.104.026211;
RA Fatland B.L., Nikolau B.J., Wurtele E.S.;
RT "Reverse genetic characterization of cytosolic acetyl-CoA generation by
RT ATP-citrate lyase in Arabidopsis.";
RL Plant Cell 17:182-203(2005).
CC -!- FUNCTION: ATP citrate-lyase is the primary enzyme responsible for the
CC synthesis of cytosolic acetyl-CoA, used for the elongation of fatty
CC acids and biosynthesis of isoprenoids, flavonoids and malonated
CC derivatives. May supply substrate to the cytosolic acetyl-CoA
CC carboxylase, which generates the malonyl-CoA used for the synthesis of
CC a multitude of compounds, including very long chain fatty acids and
CC flavonoids. Required for normal growth and development and elongation
CC of C18 fatty acids to C20 to C24 fatty acids in seeds. In contrast to
CC all known animal ACL enzymes having a homomeric structure, plant ACLs
CC are composed of alpha and beta chains. {ECO:0000269|PubMed:12376641,
CC ECO:0000269|PubMed:15608338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains.
CC {ECO:0000269|PubMed:12376641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12376641}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SGY2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in trichomes, epidermal leaf cells,
CC anther tapetal cells, stigma and in young vascular bundles of expanding
CC leaves, cotyledons, roots, pedicel of flowers and siliques.
CC {ECO:0000269|PubMed:12376641}.
CC -!- DEVELOPMENTAL STAGE: Expressed in flower buds at stage 6 of development
CC in tapetal cells and at stage 10 in the epidermal cells of growing
CC petals and ovaries. In young siliques, expressed transiently in the
CC inner integument of the ovules just prior to testal deposition.
CC Expressed in the developing embryo with a maximal level at the heart
CC and torpedo stages. The expression then disappears in the mature
CC embryo. During seed germination, expressed in the vascular bundles,
CC apical meristem, epidermis of the seedling cotyledon, stem, and root.
CC Highly expressed in the root tip of seedlings 4 days after imbibition.
CC {ECO:0000269|PubMed:12376641}.
CC -!- MISCELLANEOUS: Plants silencing ACLA-1 show a severe dwarf and dark-
CC green phenotype with some seedling lethal plants, reduced leaf cell
CC size, altered cellular ultrastructure, altered plastid ultrastructure,
CC hyperaccumulation of starch, increased accumulation of anthocyanins,
CC chlorophylls and carotenoids in vegetative organs and decreased
CC accumulation of epicuticular and cuticular waxes. These phenotypes can
CC be complemented by exogenous supply of malonate.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94933.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AY056593; AAL25637.1; -; mRNA.
DR EMBL; AC009398; AAF17657.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28624.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28625.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28627.1; -; Genomic_DNA.
DR EMBL; AY056213; AAL07062.1; -; mRNA.
DR EMBL; AY094479; AAM19846.1; -; mRNA.
DR EMBL; AY113979; AAM45027.1; -; mRNA.
DR EMBL; AK222079; BAD94933.1; ALT_INIT; mRNA.
DR EMBL; AK230271; BAF02073.1; -; mRNA.
DR EMBL; AY087536; AAM65078.1; -; mRNA.
DR RefSeq; NP_001184954.1; NM_001198025.1. [Q9SGY2-1]
DR RefSeq; NP_172537.1; NM_100943.4. [Q9SGY2-1]
DR RefSeq; NP_849634.1; NM_179303.4. [Q9SGY2-1]
DR AlphaFoldDB; Q9SGY2; -.
DR SMR; Q9SGY2; -.
DR BioGRID; 22850; 1.
DR STRING; 3702.AT1G10670.3; -.
DR iPTMnet; Q9SGY2; -.
DR PaxDb; Q9SGY2; -.
DR PRIDE; Q9SGY2; -.
DR ProteomicsDB; 244643; -. [Q9SGY2-1]
DR EnsemblPlants; AT1G10670.1; AT1G10670.1; AT1G10670. [Q9SGY2-1]
DR EnsemblPlants; AT1G10670.2; AT1G10670.2; AT1G10670. [Q9SGY2-1]
DR EnsemblPlants; AT1G10670.4; AT1G10670.4; AT1G10670. [Q9SGY2-1]
DR GeneID; 837610; -.
DR Gramene; AT1G10670.1; AT1G10670.1; AT1G10670. [Q9SGY2-1]
DR Gramene; AT1G10670.2; AT1G10670.2; AT1G10670. [Q9SGY2-1]
DR Gramene; AT1G10670.4; AT1G10670.4; AT1G10670. [Q9SGY2-1]
DR KEGG; ath:AT1G10670; -.
DR Araport; AT1G10670; -.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_3_1_1; -.
DR InParanoid; Q9SGY2; -.
DR OMA; VEMSGCR; -.
DR PhylomeDB; Q9SGY2; -.
DR BioCyc; MetaCyc:AT1G10670-MON; -.
DR PRO; PR:Q9SGY2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGY2; baseline and differential.
DR Genevisible; Q9SGY2; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.261; -; 1.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR032263; Citrate-bd.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF16114; Citrate_bind; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; ATP-binding; Cytoplasm;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..423
FT /note="ATP-citrate synthase alpha chain protein 1"
FT /id="PRO_0000412215"
FT BINDING 343
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250"
FT CONFLICT 232
FT /note="D -> Y (in Ref. 6; AAM65078)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="G -> R (in Ref. 6; AAM65078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 46679 MW; B8C5C4890A58715B CRC64;
MARKKIREYD SKRLVKEHFK RLSGKELPIR SVQINETTDL NELVEKEPWL SSEKLVVKPD
MLFGKRGKSG LVALKLDFAD VATFVKERLG KEVEMSGCKG PITTFIVEPF VPHNEEYYLN
VVSDRLGCSI SFSECGGIEI EENWDKVKTI FLPTGASLTP EICAPLVATL PLEIKAEIEE
FIKVIFTLFQ DLDFTFLEMN PFTLVDGSPY PLDMRGELDD TAAFKNFKKW GDIEFPLPFG
RVMSPTESFI HGLDEKTSAS LKFTVLNPKG RIWTMVAGGG ASVIYADTVG DLGYASELGN
YAEYSGAPKE DEVLQYARVV IDCATANPDG KSRALVIGGG IANFTDVAAT FNGIIRALKE
KEAKLKAARM HIFVRRGGPN YQKGLAKMRA LGDDIGVPIE VYGPEATMTG ICKEAIQYIT
AAA
