ACLA2_ORYSJ
ID ACLA2_ORYSJ Reviewed; 423 AA.
AC Q2QZ86; A0A0P0Y621; Q2QZ87;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
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=Os11g0696200, LOC_Os11g47330;
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 MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(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. 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=ABA95549.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000010; ABA95548.2; -; Genomic_DNA.
DR EMBL; DP000010; ABA95549.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014967; BAT15348.1; -; Genomic_DNA.
DR EMBL; AK069911; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q2QZ86; -.
DR SMR; Q2QZ86; -.
DR STRING; 4530.OS11T0696200-01; -.
DR PaxDb; Q2QZ86; -.
DR EnsemblPlants; Os11t0696200-01; Os11t0696200-01; Os11g0696200.
DR Gramene; Os11t0696200-01; Os11t0696200-01; Os11g0696200.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_3_1_1; -.
DR InParanoid; Q2QZ86; -.
DR OMA; MASEACA; -.
DR BRENDA; 2.3.3.8; 8948.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR Genevisible; Q2QZ86; 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; -; 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_0000412219"
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 409
FT /note="T -> A (in Ref. 5; AK069911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 46542 MW; 434D4C43D17AA2C7 CRC64;
MARKKIREYD SKRLLKEHLK RLAGIDLQIL SAQVTQSTDF TELVNQQPWL STMKLVVKPD
MLFGKRGKSG LVALNLDIAQ VKEFVKERLG VEVEMGGCKA PITTFIVEPF VPHDQEYYLS
IVSERLGSTI SFSECGGIEI EENWDKVKTI FLPTEKPMTP DACAPLIATL PLEARGKIGD
FIKGVFAVFQ DLDFSFLEMN PFTIVNGEPY PLDMRGELDD TAAFKNFKKW GNIEFPLPFG
RVLSSTEGFI HDLDEKTSAS LKFTVLNPKG RIWTMVAGGG ASVIYADTVG DLGYASELGN
YAEYSGAPNE EEVLQYARVV LDCATADPDG RKRALLIGGG IANFTDVGAT FSGIIRALRE
KESKLKAARM HIYVRRGGPN YQTGLAKMRK LGAELGVPIE VYGPEATMTG ICKQAIECVM
AAA
