ACLA3_ARATH
ID ACLA3_ARATH Reviewed; 424 AA.
AC O80526;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ATP-citrate synthase alpha chain protein 3;
DE Short=ATP-citrate synthase A-3;
DE EC=2.3.3.8;
DE AltName: Full=ATP-citrate lyase A-3;
DE AltName: Full=Citrate cleavage enzyme A-3;
GN Name=ACLA-3; OrderedLocusNames=At1g09430; ORFNames=F19J9.9;
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 [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 [2]
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 [3]
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).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; AC003970; AAC33203.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28442.1; -; Genomic_DNA.
DR EMBL; AY127019; AAM83243.1; -; mRNA.
DR EMBL; BT003017; AAO23582.1; -; mRNA.
DR PIR; F86227; F86227.
DR RefSeq; NP_172414.1; NM_100814.4.
DR AlphaFoldDB; O80526; -.
DR SMR; O80526; -.
DR BioGRID; 22707; 1.
DR IntAct; O80526; 1.
DR STRING; 3702.AT1G09430.1; -.
DR iPTMnet; O80526; -.
DR PaxDb; O80526; -.
DR PRIDE; O80526; -.
DR ProteomicsDB; 244644; -.
DR EnsemblPlants; AT1G09430.1; AT1G09430.1; AT1G09430.
DR GeneID; 837466; -.
DR Gramene; AT1G09430.1; AT1G09430.1; AT1G09430.
DR KEGG; ath:AT1G09430; -.
DR Araport; AT1G09430; -.
DR TAIR; locus:2012310; AT1G09430.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_3_1_1; -.
DR InParanoid; O80526; -.
DR OMA; ANGRVWT; -.
DR OrthoDB; 628176at2759; -.
DR PhylomeDB; O80526; -.
DR PRO; PR:O80526; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80526; baseline and differential.
DR Genevisible; O80526; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; ISS:TAIR.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; TAS:TAIR.
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 2: Evidence at transcript level;
KW Acyltransferase; ATP-binding; Cytoplasm; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..424
FT /note="ATP-citrate synthase alpha chain protein 3"
FT /id="PRO_0000412217"
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"
SQ SEQUENCE 424 AA; 46946 MW; FE9AFB8E6CB67389 CRC64;
MARKKIREYD SKRLLKEHLK RLANIDLQIR SAQVTESTDF TELTNQESWL SSTKLVVKPD
MLFGKRGKSG LVALKLDLAE VADFVKARLG TEVEMEGCKA PITTFIVEPF VPHDQEYYLS
IVSDRLGCTI SFSECGGIEI EENWDKVKTI FLPAEKSMTL EVCAPLIATL PLEVRAKIGN
FIMGAFAVFQ DLDFSFMEMN PFTLVDGEPF PLDMRGELDD TAAFKNFNKW GDIEFPLPFG
RVLSSTENFI HGLDEKTSAS LKFTVLNPKG RIWTMVAGGG ASVIYADTVG DLGYASELGN
YAEYSGAPNE EEVLQYARVV IDCATTDPDG RKRALLIGGG IANFTDVAAT FNGIIRALRE
KETRLKASRM HIYVRRGGPN YQTGLARMRA LGEELGVPLE VYGPEATMTG ICKRAIDCIM
LPDA
