ID ACLB2_ARATH Reviewed; 608 AA.
AC Q9FGX1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=ATP-citrate synthase beta chain protein 2 {ECO:0000303|PubMed:12376641};
DE Short=ATP-citrate synthase B-2 {ECO:0000303|PubMed:12376641};
DE EC=2.3.3.8 {ECO:0000269|PubMed:12376641};
DE AltName: Full=ATP-citrate lyase B-2 {ECO:0000303|PubMed:12376641};
DE AltName: Full=Citrate cleavage enzyme B-2 {ECO:0000303|PubMed:12376641};
GN Name=ACLB-2 {ECO:0000303|PubMed:12376641};
GN OrderedLocusNames=At5g49460 {ECO:0000312|Araport:AT5G49460};
GN ORFNames=K7J8.14 {ECO:0000312|EMBL:BAB09916.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, 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).
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. n 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 -!- 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 Evidence={ECO:0000269|PubMed:12376641};
CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains.
CC {ECO:0000305|PubMed:12376641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12376641}.
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 -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; AB023034; BAB09916.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95814.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70656.1; -; Genomic_DNA.
DR EMBL; AY035067; AAK59572.1; -; mRNA.
DR EMBL; AY056594; AAL25638.1; -; mRNA.
DR EMBL; AY062956; AAL33788.1; -; mRNA.
DR RefSeq; NP_001332247.1; NM_001344844.1.
DR RefSeq; NP_199757.1; NM_124323.4.
DR AlphaFoldDB; Q9FGX1; -.
DR SMR; Q9FGX1; -.
DR BioGRID; 20252; 6.
DR STRING; 3702.Q9FGX1; -.
DR iPTMnet; Q9FGX1; -.
DR PaxDb; 3702-AT5G49460-1; -.
DR ProteomicsDB; 244368; -.
DR EnsemblPlants; AT5G49460.1; AT5G49460.1; AT5G49460.
DR EnsemblPlants; AT5G49460.2; AT5G49460.2; AT5G49460.
DR GeneID; 835006; -.
DR Gramene; AT5G49460.1; AT5G49460.1; AT5G49460.
DR Gramene; AT5G49460.2; AT5G49460.2; AT5G49460.
DR KEGG; ath:AT5G49460; -.
DR Araport; AT5G49460; -.
DR TAIR; AT5G49460; ACLB-2.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_4_2_1; -.
DR InParanoid; Q9FGX1; -.
DR OMA; HMLRYQA; -.
DR OrthoDB; 536at2759; -.
DR PhylomeDB; Q9FGX1; -.
DR BioCyc; MetaCyc:AT5G49460-MONOMER; -.
DR PRO; PR:Q9FGX1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGX1; baseline and differential.
DR Genevisible; Q9FGX1; AT.
DR GO; GO:0140615; C:ATP-dependent citrate lyase complex; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; TAS:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd06100; CCL_ACL-C; 1.
DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR PANTHER; PTHR23118:SF42; ATP-CITRATE SYNTHASE; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PRINTS; PR01798; SCOASYNTHASE.
DR SUPFAM; SSF48256; Citrate synthase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; ATP-binding; Cytoplasm; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..608
FT /note="ATP-citrate synthase beta chain protein 2"
FT /id="PRO_0000412222"
FT ACT_SITE 273
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P16638"
FT BINDING 214..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P53585"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q84LB6"
FT BINDING 265..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P53585"
FT BINDING 292..302
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255"
SQ SEQUENCE 608 AA; 65828 MW; B5594BBD3D93BCBC CRC64;
MATGQLFSRT TQALFYNYKQ LPVQRMLDFD FLCGRETPSV AGIINPGSEG FQKLFFGQEE
IAIPVHAAIE AACAAHPTAD VFINFASFRS AAASSMAALK QPTIKVVAII AEGVPESDTK
QLIAYARANN KVVIGPATVG GIQAGAFKIG DTAGTIDNII QCKLYRPGSV GFVSKSGGMS
NEMYNTVARV TDGIYEGIAI GGDVFPGSTL SDHILRFNNI PQIKMMVVLG ELGGRDEYSL
VEALKEGKVN KPVVAWVSGT CARLFKSEVQ FGHAGAKSGG EMESAQAKNQ ALIDAGAIVP
TSFEALESAI KETFEKLVEE GKVSPIKEVI PPQIPEDLNS AIKSGKVRAP THIISTISDD
RGEEPCYAGV PMSSIIEQGY GVGDVISLLW FKRSLPRYCT KFIEICIMLC ADHGPCVSGA
HNTIVTARAG KDLVSSLVSG LLTIGPRFGG AIDDAARYFK DACDRNLTPY EFVEGMKKKG
IRVPGIGHRI KSRDNRDKRV ELLQKFARSN FPSVKYMEYA VTVETYTLSK ANNLVLNVDG
AIGSLFLDLL AGSGMFTKQE IDEIVQIGYL NGLFVLARSI GLIGHTFDQK RLKQPLYRHP
WEDVLYTK
//
