ID   ACLA1_ORYSJ             Reviewed;         407 AA.
AC   Q53JY8; C7J931; Q53QC5;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=ATP-citrate synthase subunit 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=Os11g0693800, LOC_Os11g47120;
GN   ORFNames=OsJ_34825;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(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. In contrast to all known animal ACL enzymes having a
CC       homomeric structure, plant ACLs are composed of alpha and beta chains
CC       (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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX95006.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAX96579.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABA95455.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAH95456.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAZ19281.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC116367; AAX96579.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC146937; AAX95006.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000010; ABA95455.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008217; BAH95456.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000148; EAZ19281.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q53JY8; -.
DR   SMR; Q53JY8; -.
DR   STRING; 39947.Q53JY8; -.
DR   PaxDb; Q53JY8; -.
DR   PRIDE; Q53JY8; -.
DR   InParanoid; Q53JY8; -.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000007752; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
DR   Genevisible; Q53JY8; OS.
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; -; 2.
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; 2.
DR   SUPFAM; SSF52210; SSF52210; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ATP-binding; Cytoplasm; Lipid biosynthesis;
KW   Lipid metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..407
FT                   /note="ATP-citrate synthase subunit alpha chain protein 1"
FT                   /id="PRO_0000412218"
FT   BINDING         327
FT                   /ligand="citrate"
FT                   /ligand_id="ChEBI:CHEBI:16947"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="citrate"
FT                   /ligand_id="ChEBI:CHEBI:16947"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="citrate"
FT                   /ligand_id="ChEBI:CHEBI:16947"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   407 AA;  45005 MW;  73BE1231A0BC6718 CRC64;
     MARKKIREYD SKRLLKEHLK RLAGIDLQIL SAQVTQSTDF TELVNQQPWL STMKLVVKPD
     MLFGKRGKSG LVALNLDIAQ VKEFVKERLG VEVEMGGCKA PITTFIVEPF VPHDQEYYLS
     IVSERLGSTI SFSECGGIEI EENWDKVKTI FLSTEKPMTP DACAPLIATL PLEARGKIGD
     FIKGVFAVFQ DLDFSFLEMN PFTIVNGEPY PLDMRGELDD TAAFKTSRSK WGNIEFPLPF
     GRVLSSTEGF IHDLDEKTSA SLKFTVLNPK GRIWTMVAGG ELENYAEYSG APNEEEVLQY
     ARVVLDCATA DPDGRKRALL IGGGIANFTD VGATFSGIIR ALREKESKLK AARMHIYVRR
     GGPNYQTGLA KMRKLGAELG VPIEVYGPEA TMTGICKQAI ECVMAAA