ACO2M_ARATH
ID ACO2M_ARATH Reviewed; 995 AA.
AC Q94A28; Q9SZ36;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Aconitate hydratase 2, mitochondrial {ECO:0000303|PubMed:25061985};
DE Short=Aconitase 2 {ECO:0000303|PubMed:25061985};
DE Short=mACO2 {ECO:0000303|PubMed:24296071};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:P19414};
DE AltName: Full=Citrate hydro-lyase 2 {ECO:0000303|PubMed:25061985};
DE Flags: Precursor;
GN Name=ACO2 {ECO:0000303|PubMed:25061985};
GN OrderedLocusNames=At4g26970 {ECO:0000312|Araport:AT4G26970};
GN ORFNames=F10M23.310 {ECO:0000312|EMBL:CAB36543.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, RESPONSE TO IRON STARVATION, AND
RP 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 [5]
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 [6]
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [8]
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).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. Contributes to oxidative stress tolerance (PubMed:17013749).
CC Involved in acetate assimilation (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. {ECO:0000250|UniProtKB:P20004}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, leaves and flowers, also
CC present in stems, and, at low levels, in seeds.
CC {ECO:0000269|PubMed:17437406}.
CC -!- INDUCTION: Slight level decrease after 3 days of iron starvation.
CC {ECO:0000269|PubMed:17437406}.
CC -!- DISRUPTION PHENOTYPE: Reduced mitochondrial aconitase (ACO) activity by
CC 20 percent (PubMed:17013749, PubMed:17437406). Increased tolerance to
CC oxidative stress mediated by paraquat, a superoxide-generating agent
CC (PubMed:17013749). Altered acetate assimilation leading to lower levels
CC of CO(2), CHO and SO, and higher OAs (organic acids) accumulation,
CC especially fumarate (PubMed:25061985). {ECO:0000269|PubMed:17013749,
CC ECO:0000269|PubMed:17437406, ECO:0000269|PubMed:25061985}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36543.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79552.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035440; CAB36543.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161566; CAB79552.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85279.1; -; Genomic_DNA.
DR EMBL; AY050431; AAK91447.1; -; mRNA.
DR EMBL; BT000492; AAN18061.1; -; mRNA.
DR PIR; T04820; T04820.
DR RefSeq; NP_567763.2; NM_118831.4.
DR AlphaFoldDB; Q94A28; -.
DR SMR; Q94A28; -.
DR BioGRID; 14092; 5.
DR STRING; 3702.AT4G26970.1; -.
DR iPTMnet; Q94A28; -.
DR MetOSite; Q94A28; -.
DR PaxDb; Q94A28; -.
DR PRIDE; Q94A28; -.
DR ProteomicsDB; 244750; -.
DR EnsemblPlants; AT4G26970.1; AT4G26970.1; AT4G26970.
DR GeneID; 828805; -.
DR Gramene; AT4G26970.1; AT4G26970.1; AT4G26970.
DR KEGG; ath:AT4G26970; -.
DR Araport; AT4G26970; -.
DR TAIR; locus:2116297; AT4G26970.
DR eggNOG; KOG0452; Eukaryota.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; Q94A28; -.
DR OMA; LRSFRVC; -.
DR OrthoDB; 190960at2759; -.
DR UniPathway; UPA00223; UER00718.
DR PRO; PR:Q94A28; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94A28; baseline and differential.
DR Genevisible; Q94A28; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; 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: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:TAIR.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; IMP:TAIR.
DR GO; GO:1990641; P:response to iron ion starvation; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
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; Glyoxylate bypass; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..83
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 84..995
FT /note="Aconitate hydratase 2, mitochondrial"
FT /id="PRO_0000259922"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 306..308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 538
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 604
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 607
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 637
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 642
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 800
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 881..882
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT CONFLICT 407
FT /note="T -> A (in Ref. 3; AAK91447/AAN18061)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="D -> E (in Ref. 1; CAB36543/CAB79552)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="E -> G (in Ref. 3; AAK91447/AAN18061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 995 AA; 108481 MW; 20FC18030F1CBDDB CRC64;
MYRRATSGVR SASARLSSSL SRIASSETAS VSAPSASSLR NQTNRSKSFS SALRSFRVCS
ASTRWSHGGS WGSPASLRAQ ARNSTPVMEK FERKYATMAS EHSYKDILTS LPKPGGGEYG
KYYSLPALND PRIDKLPFSV RILLESAIRN CDNYQVTKDD VEKILDWENT STKQVEIAFK
PARVILQDFT GVPVLVDLAS MRDAVKNLGS DPSKINPLVP VDLVVDHSIQ VDFARSEDAA
QKNLELEFKR NKERFTFLKW GSTAFQNMLV VPPGSGIVHQ VNLEYLGRVV FNSKGFLYPD
SVVGTDSHTT MIDGLGVAGW GVGGIEAEAA MLGQPMSMVL PGVVGFKLDG KLKEGVTATD
LVLTVTQILR KHGVVGKFVE FYGEGMSELS LADRATIANM SPEYGATMGF FPVDHVTLEY
LKLTGRSDET VSMIESYLRA NNMFVDYNEP QQERAYTSYL QLDLGHVEPC ISGPKRPHDR
VPLKDMKADW HACLDNPVGF KGFAVPKEKQ EEVVKFSYNG QPAEIKHGSV VIAAITSCTN
TSNPSVMIGA ALVAKKASDL GLKVKPWVKT SLAPGSRVVE KYLDRSGLRE SLTKQGFEIV
GYGCTTCIGN SGNLDPEVAS AIEGTDIIPA AVLSGNRNFE GRVHPQTRAN YLASPPLVVA
YALAGTVDID FEKEPIGTRS DGKSVYLRDV WPSNEEVAQV VQYSVLPSMF KSSYETITEG
NPLWNELSAP SSTLYSWDPN STYIHEPPYF KNMTANPPGP REVKDAYCLL NFGDSVTTDH
ISPAGNIQKT SPAAKFLMDR GVISEDFNSY GSRRGNDEVM ARGTFANIRI VNKLLKGEVG
PNTVHIPTGE KLSVFDAASK YKTAEQDTII LAGAEYGSGS SRDWAAKGPL LLGVKAVIAK
SFERIHRSNL AGMGIIPLCF KAGEDAETLG LTGHERYTVH LPTKVSDIRP GQDVTVTTDS
GKSFVCTLRF DTEVELAYYD HGGILPYVIR SLSAK
