ACO3M_ARATH
ID ACO3M_ARATH Reviewed; 990 AA.
AC Q9SIB9; Q8L784;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Aconitate hydratase 3, mitochondrial {ECO:0000303|PubMed:25061985};
DE Short=Aconitase 3 {ECO:0000303|PubMed:25061985};
DE Short=mACO1 {ECO:0000303|PubMed:24296071};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:P19414};
DE AltName: Full=Citrate hydro-lyase 3 {ECO:0000303|PubMed:25061985};
DE Flags: Precursor;
GN Name=ACO3 {ECO:0000303|PubMed:25061985};
GN OrderedLocusNames=At2g05710 {ECO:0000312|Araport:AT2G05710};
GN ORFNames=T3P4.5 {ECO:0000312|EMBL:AAD25640.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [5]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17437406; DOI=10.1042/bj20061874;
RA Arnaud N., Ravet K., Borlotti A., Touraine B., Boucherez J., Fizames C.,
RA Briat J.F., Cellier F., Gaymard F.;
RT "The iron-responsive element (IRE)/iron-regulatory protein 1 (IRP1)-
RT cytosolic aconitase iron-regulatory switch does not operate in plants.";
RL Biochem. J. 405:523-531(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17013749; DOI=10.1007/s11103-006-9087-x;
RA Moeder W., Del Pozo O., Navarre D.A., Martin G.B., Klessig D.F.;
RT "Aconitase plays a role in regulating resistance to oxidative stress and
RT cell death in Arabidopsis and Nicotiana benthamiana.";
RL Plant Mol. Biol. 63:273-287(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION DURING
RP GERMINATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25061985; DOI=10.1042/bj20140430;
RA Hooks M.A., Allwood J.W., Harrison J.K., Kopka J., Erban A., Goodacre R.,
RA Balk J.;
RT "Selective induction and subcellular distribution of ACONITASE 3 reveal the
RT importance of cytosolic citrate metabolism during lipid mobilization in
RT Arabidopsis.";
RL Biochem. J. 463:309-317(2014).
RN [9]
RP GENE FAMILY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24296071; DOI=10.1104/pp.113.225524;
RA Taylor N.L., Fenske R., Castleden I., Tomaz T., Nelson C.J., Millar A.H.;
RT "Selected reaction monitoring to determine protein abundance in Arabidopsis
RT using the Arabidopsis proteotypic predictor.";
RL Plant Physiol. 164:525-536(2014).
RN [10]
RP INTERACTION WITH B'GAMMA, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION AT SER-91.
RC STRAIN=cv. Columbia;
RX PubMed=25307043; DOI=10.1111/nph.13097;
RA Konert G., Trotta A., Kouvonen P., Rahikainen M., Durian G., Blokhina O.,
RA Fagerstedt K., Muth D., Corthals G.L., Kangasjaervi S.;
RT "Protein phosphatase 2A (PP2A) regulatory subunit B'gamma interacts with
RT cytoplasmic ACONITASE 3 and modulates the abundance of AOX1A and AOX1D in
RT Arabidopsis thaliana.";
RL New Phytol. 205:1250-1263(2015).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. Contributes to oxidative stress tolerance (PubMed:17013749).
CC Modulates cytosolic citrate metabolism during lipid mobilization.
CC Required during seedling growth (PubMed:25061985).
CC {ECO:0000269|PubMed:17013749, ECO:0000269|PubMed:25061985}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:P19414};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P20004};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P20004};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:P19414}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with B'GAMMA in the cytosol
CC (PubMed:25307043). {ECO:0000250|UniProtKB:P20004,
CC ECO:0000269|PubMed:25307043}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:25061985}. Cytoplasm {ECO:0000269|PubMed:25061985,
CC ECO:0000269|PubMed:25307043}. Note=Cytosolic localization in 3-day-old
CC seedlings, but mitochondrial in 10-day-old plantlets.
CC {ECO:0000269|PubMed:25061985}.
CC -!- TISSUE SPECIFICITY: Major aconitase isoenzyme in young seedlings
CC (PubMed:25061985). Expressed in roots, leaves, stems and flowers, and,
CC at low levels, in seeds (PubMed:17437406).
CC {ECO:0000269|PubMed:17437406, ECO:0000269|PubMed:25061985}.
CC -!- INDUCTION: Transiently induced during germination.
CC {ECO:0000269|PubMed:25061985}.
CC -!- PTM: Phosphorylated at Ser-91 in the cytoplasm; this phosphorylation
CC requires the presence of B'GAMMA. {ECO:0000269|PubMed:25307043}.
CC -!- DISRUPTION PHENOTYPE: Reduced cytosolic and mitochondrial aconitase
CC (ACO) activities by 25 and 55 precent, respectively (PubMed:17013749,
CC PubMed:17437406). Increased tolerance to oxidative stress mediated by
CC paraquat, a superoxide-generating agent (PubMed:17013749). Delayed
CC early seedling growth, altered assimilation of acetate feeding and
CC elevated citrate and malate levels (PubMed:25061985).
CC {ECO:0000269|PubMed:17013749, ECO:0000269|PubMed:17437406,
CC ECO:0000269|PubMed:25061985}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25640.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007170; AAD25640.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC05964.1; -; Genomic_DNA.
DR EMBL; AY136414; AAM97080.1; -; mRNA.
DR EMBL; BT008809; AAP68248.1; -; mRNA.
DR PIR; B84471; B84471.
DR RefSeq; NP_178634.2; NM_126589.3.
DR AlphaFoldDB; Q9SIB9; -.
DR SMR; Q9SIB9; -.
DR BioGRID; 519; 23.
DR IntAct; Q9SIB9; 1.
DR STRING; 3702.AT2G05710.1; -.
DR iPTMnet; Q9SIB9; -.
DR MetOSite; Q9SIB9; -.
DR PaxDb; Q9SIB9; -.
DR PRIDE; Q9SIB9; -.
DR ProteomicsDB; 243283; -.
DR EnsemblPlants; AT2G05710.1; AT2G05710.1; AT2G05710.
DR GeneID; 815120; -.
DR Gramene; AT2G05710.1; AT2G05710.1; AT2G05710.
DR KEGG; ath:AT2G05710; -.
DR Araport; AT2G05710; -.
DR TAIR; locus:2063354; AT2G05710.
DR eggNOG; KOG0452; Eukaryota.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; Q9SIB9; -.
DR OMA; ACQRYNM; -.
DR OrthoDB; 190960at2759; -.
DR PhylomeDB; Q9SIB9; -.
DR BRENDA; 4.2.1.3; 399.
DR UniPathway; UPA00223; UER00718.
DR PRO; PR:Q9SIB9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIB9; baseline and differential.
DR Genevisible; Q9SIB9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0030350; F:iron-responsive element binding; IBA:GO_Central.
DR GO; GO:0006101; P:citrate metabolic process; IMP:UniProtKB.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0090351; P:seedling development; IMP:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01341; aconitase_1; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Glyoxylate bypass; Iron; Iron-sulfur; Lyase;
KW Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..78
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 79..990
FT /note="Aconitate hydratase 3, mitochondrial"
FT /id="PRO_0000259921"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 301..303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 533
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 599
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 602
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 632
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 637
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 795
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 876..877
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25307043"
SQ SEQUENCE 990 AA; 108201 MW; 552AE563BC2981ED CRC64;
MYLTASSSAS SSIIRAASSR SSSLFSFRSV LSPSVSSTSP SSLLARRSFG TISPAFRRWS
HSFHSKPSPF RFTSQIRAVS PVLDRLQRTF SSMASEHPFK GIFTTLPKPG GGEFGKFYSL
PALNDPRVDK LPYSIRILLE SAIRNCDNFQ VTKEDVEKII DWEKTSPKQV EIPFKPARVL
LQDFTGVPAV VDLACMRDAM NKLGSDSNKI NPLVPVDLVI DHSVQVDVAR SENAVQANME
LEFQRNKERF AFLKWGSTAF QNMLVVPPGS GIVHQVNLEY LGRVVFNTKG LLYPDSVVGT
DSHTTMIDGL GVAGWGVGGI EAEATMLGQP MSMVLPGVVG FKLAGKMRNG VTATDLVLTV
TQMLRKHGVV GKFVEFYGNG MSGLSLADRA TIANMSPEYG ATMGFFPVDH VTLQYLKLTG
RSDETVAMIE AYLRANNMFV DYNEPQQDRV YSSYLELNLD DVEPCISGPK RPHDRVTLKE
MKADWHSCLD SKVGFKGFAI PKEAQEKVVN FSFDGQPAEL KHGSVVIAAI TSCTNTSNPS
VMLGAGLVAK KACDLGLQVK PWIKTSLAPG SGVVTKYLLK SGLQEYLNEQ GFNIVGYGCT
TCIGNSGEIN ESVGAAITEN DIVAAAVLSG NRNFEGRVHP LTRANYLASP PLVVAYALAG
TVNIDFETEP IGKGKNGKDV FLRDIWPTTE EIAEVVQSSV LPDMFRATYE SITKGNPMWN
KLSVPENTLY SWDPNSTYIH EPPYFKDMTM DPPGPHNVKD AYCLLNFGDS ITTDHISPAG
NIQKDSPAAK FLMERGVDRK DFNSYGSRRG NDEIMARGTF ANIRIVNKLM NGEVGPKTVH
IPSGEKLSVF DAAMRYKSSG EDTIILAGAE YGSGSSRDWA AKGPMLQGVK AVIAKSFERI
HRSNLVGMGI IPLCFKSGED ADTLGLTGHE RYTIHLPTDI SEIRPGQDVT VTTDNGKSFT
CTVRFDTEVE LAYFNHGGIL PYVIRNLSKQ
