ACLA2_ARATH
ID ACLA2_ARATH Reviewed; 423 AA.
AC O22718; Q8RXG2; Q9C6C0;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=ATP-citrate synthase alpha chain protein 2;
DE Short=ATP-citrate synthase A-2;
DE EC=2.3.3.8;
DE AltName: Full=ATP-citrate lyase A-2;
DE AltName: Full=Citrate cleavage enzyme A-2;
GN Name=ACLA-2; OrderedLocusNames=At1g60810; ORFNames=F23C21.5, F8A5.32;
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; AC002292; AAB71965.1; -; Genomic_DNA.
DR EMBL; AC079675; AAG51870.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33735.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58113.1; -; Genomic_DNA.
DR EMBL; AY081273; AAL91162.1; -; mRNA.
DR EMBL; AY128741; AAM91141.1; -; mRNA.
DR PIR; F96633; F96633.
DR RefSeq; NP_001320572.1; NM_001333917.1.
DR RefSeq; NP_176280.1; NM_104764.4.
DR AlphaFoldDB; O22718; -.
DR SMR; O22718; -.
DR BioGRID; 27599; 1.
DR STRING; 3702.AT1G60810.1; -.
DR PaxDb; O22718; -.
DR PRIDE; O22718; -.
DR ProteomicsDB; 243282; -.
DR DNASU; 842375; -.
DR EnsemblPlants; AT1G60810.1; AT1G60810.1; AT1G60810.
DR EnsemblPlants; AT1G60810.2; AT1G60810.2; AT1G60810.
DR GeneID; 842375; -.
DR Gramene; AT1G60810.1; AT1G60810.1; AT1G60810.
DR Gramene; AT1G60810.2; AT1G60810.2; AT1G60810.
DR KEGG; ath:AT1G60810; -.
DR Araport; AT1G60810; -.
DR TAIR; locus:2025865; AT1G60810.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_3_1_1; -.
DR InParanoid; O22718; -.
DR OMA; HIEENWD; -.
DR OrthoDB; 628176at2759; -.
DR PhylomeDB; O22718; -.
DR PRO; PR:O22718; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O22718; baseline and differential.
DR Genevisible; O22718; AT.
DR GO; GO:0140615; C:ATP-dependent citrate lyase complex; ISS:TAIR.
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; 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..423
FT /note="ATP-citrate synthase alpha chain protein 2"
FT /id="PRO_0000412216"
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 156
FT /note="A -> P (in Ref. 3; AAL91162/AAM91141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 46760 MW; E1F9F2A765090F70 CRC64;
MARKKIREYD SKRLVKEHFK RLSGQELPIR SVQINQETDL NELVEREPWL SSEKLVVKPD
MLFGKRGKSG LVALNLDFAD VATFVKERLG KEVEMSGCKG PITTFIVEPF VPHNEEFYLN
IVSDRLGCSI SFSECGGIDI EENWDKVKTI TIPTGASLTF EICAPLVATL PLEIKGELED
FIQVIFTLFE DLDFTFLEMN PFTLVDGKPY PLDMRGELDD TAAFKNFKKW GDIEFPMPFG
RVMSSTESFI HGLDEKTSAS LKFTVLNPKG RIWTMVAGGG ASVIYADTVG DLGYASELGN
YAEYSGAPKE DEVLQYARVV IDCATANPDG KSRALVIGGG IANFTDVAAT FNGIIRALKE
KEAKLKAARM HIFVRRGGPN YQKGLAKMRS LGDEIGVPIE VYGPEATMTG ICKEAIQYIT
AAA
