ACLB1_ARATH
ID ACLB1_ARATH Reviewed; 608 AA.
AC Q9C522;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ATP-citrate synthase beta chain protein 1;
DE Short=ATP-citrate synthase B-1;
DE EC=2.3.3.8;
DE AltName: Full=ATP-citrate lyase B-1;
DE AltName: Full=Citrate cleavage enzyme B-1;
GN Name=ACLB-1; OrderedLocusNames=At3g06650; ORFNames=F5E6.2, T8E24.7;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; AC020580; AAG51326.1; -; Genomic_DNA.
DR EMBL; AC036106; AAG50997.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74426.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64284.1; -; Genomic_DNA.
DR EMBL; BT002736; AAO22565.1; -; mRNA.
DR RefSeq; NP_001326324.1; NM_001337675.1.
DR RefSeq; NP_187317.1; NM_111541.4.
DR AlphaFoldDB; Q9C522; -.
DR SMR; Q9C522; -.
DR BioGRID; 5180; 4.
DR STRING; 3702.AT3G06650.1; -.
DR iPTMnet; Q9C522; -.
DR PaxDb; Q9C522; -.
DR PRIDE; Q9C522; -.
DR ProteomicsDB; 244358; -.
DR EnsemblPlants; AT3G06650.1; AT3G06650.1; AT3G06650.
DR EnsemblPlants; AT3G06650.2; AT3G06650.2; AT3G06650.
DR GeneID; 819845; -.
DR Gramene; AT3G06650.1; AT3G06650.1; AT3G06650.
DR Gramene; AT3G06650.2; AT3G06650.2; AT3G06650.
DR KEGG; ath:AT3G06650; -.
DR Araport; AT3G06650; -.
DR TAIR; locus:2084284; AT3G06650.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_4_2_1; -.
DR InParanoid; Q9C522; -.
DR OMA; XILASFI; -.
DR OrthoDB; 349367at2759; -.
DR PhylomeDB; Q9C522; -.
DR PRO; PR:Q9C522; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C522; baseline and differential.
DR Genevisible; Q9C522; AT.
DR GO; GO:0140615; C:ATP-dependent citrate lyase complex; ISS:TAIR.
DR GO; GO:0005829; C:cytosol; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR Gene3D; 3.40.50.261; -; 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; IPR005811; CoA_ligase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF00285; Citrate_synt; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR SUPFAM; SSF48256; SSF48256; 1.
DR SUPFAM; SSF51735; SSF51735; 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 2: Evidence at transcript 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 1"
FT /id="PRO_0000412221"
FT ACT_SITE 273
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 214..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 265..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 292..302
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255"
SQ SEQUENCE 608 AA; 65814 MW; 8AABDE96ADA2BAD6 CRC64;
MATGQLFSRN TQALFYNYKQ LPIQRMLDFD FLCGRETPSV AGIINPGSEG FQKLFFGQEE
IAIPVHAAIE AACAAHPTAD VFINFASFRS AAASSMAALK QPTIKVVAII AEGVPESDTK
QLIAYARANN KVIIGPATVG GVQAGAFKIG DTAGTIDNII QCKLYRPGSV GFVSKSGGMS
NEMYNTIARV TDGIYEGIAI GGDVFPGSTL SDHILRFNNI PQIKMVVVLG ELGGRDEYSL
VEAMKQGKVT KPVVAWVSGT CARLFKSEVQ FGHAGAKSGG EMESAQAKNQ ALQDAGATVP
TSFEALEVAI KETFDKLVEE GKVSPIKEVT PPQIPEDLSS AIKSGKVRAP THIISTISDD
RGEEPCYAGV PMSSIIEQGY GVGDVISLLW FKRSLPRYCT KFIEICIMLC ADHGPCVSGA
HNTIVTARAG KDLVSSLVSG LLTIGPRFGG AIDDAARYFK DACDRNLTPY EFVEGMKKKG
IRVPGIGHRI KSRDNRDKRV ELLQKFARSN FPAVKYMEYA VQVETYTLSK ANNLVLNVDG
AIGSLFLDLL AGSGMFTKQE IDEIVQIGYL NGLFVLARSI GLIGHTFDQK RLKQPLYRHP
WEDVLYTK
