ACO1_ARATH
ID ACO1_ARATH Reviewed; 898 AA.
AC Q42560; Q9SZT1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Aconitate hydratase 1 {ECO:0000303|PubMed:25061985};
DE Short=Aconitase 1 {ECO:0000303|PubMed:25061985};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:P19414};
DE AltName: Full=Citrate hydro-lyase 1 {ECO:0000303|PubMed:25061985};
GN Name=ACO1 {ECO:0000303|PubMed:25061985}; Synonyms=ACO;
GN OrderedLocusNames=At4g35830 {ECO:0000312|Araport:AT4G35830};
GN ORFNames=F4B14.100 {ECO:0000312|EMBL:CAA21469.1};
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Columbia;
RX PubMed=7713917; DOI=10.1074/jbc.270.14.8131;
RA Peyret P., Perez P., Alric M.;
RT "Structure, genomic organization, and expression of the Arabidopsis
RT thaliana aconitase gene. Plant aconitase show significant homology with
RT mammalian iron-responsive element-binding protein.";
RL J. Biol. Chem. 270:8131-8137(1995).
RN [2]
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 [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 44-52 AND 472-485.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
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 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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
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).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. Contributes to oxidative stress tolerance (PubMed:17013749).
CC May have a role in respiration (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: Cytoplasm {ECO:0000269|PubMed:14671022}.
CC Mitochondrion {ECO:0000269|PubMed:14671022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q42560-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, stems and leaves, also
CC present in stems and flowers. {ECO:0000269|PubMed:17437406}.
CC -!- INDUCTION: Slight level decrease after 3 days of iron starvation.
CC {ECO:0000269|PubMed:17437406}.
CC -!- DISRUPTION PHENOTYPE: Reduced cytosolic and mitochondrial aconitase
CC (ACO) activities by 70 and 20 precent, respectively (PubMed:17013749,
CC PubMed:17437406). Increased tolerance to oxidative stress mediated by
CC paraquat, a superoxide-generating agent (PubMed:17013749). Slightly
CC higher production of CO(2) (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=CAA58046.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X82839; CAA58046.1; ALT_INIT; mRNA.
DR EMBL; AL031986; CAA21469.1; -; Genomic_DNA.
DR EMBL; AL161588; CAB81492.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86576.1; -; Genomic_DNA.
DR EMBL; AY062772; AAL32850.1; -; mRNA.
DR PIR; T04693; T04693.
DR RefSeq; NP_195308.1; NM_119749.4. [Q42560-1]
DR AlphaFoldDB; Q42560; -.
DR SMR; Q42560; -.
DR BioGRID; 15019; 22.
DR IntAct; Q42560; 1.
DR STRING; 3702.AT4G35830.1; -.
DR iPTMnet; Q42560; -.
DR MetOSite; Q42560; -.
DR PaxDb; Q42560; -.
DR PRIDE; Q42560; -.
DR ProteomicsDB; 244724; -. [Q42560-1]
DR EnsemblPlants; AT4G35830.1; AT4G35830.1; AT4G35830. [Q42560-1]
DR GeneID; 829737; -.
DR Gramene; AT4G35830.1; AT4G35830.1; AT4G35830. [Q42560-1]
DR KEGG; ath:AT4G35830; -.
DR Araport; AT4G35830; -.
DR TAIR; locus:2125354; AT4G35830.
DR eggNOG; KOG0452; Eukaryota.
DR InParanoid; Q42560; -.
DR PhylomeDB; Q42560; -.
DR BioCyc; MetaCyc:AT4G35830-MON; -.
DR BRENDA; 1.14.17.4; 399.
DR UniPathway; UPA00223; UER00718.
DR PRO; PR:Q42560; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42560; baseline and differential.
DR Genevisible; Q42560; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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: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:0048027; F:mRNA 5'-UTR binding; IDA:TAIR.
DR GO; GO:0006101; P:citrate metabolic process; IMP:TAIR.
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: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; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Mitochondrion; Reference proteome; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..898
FT /note="Aconitate hydratase 1"
FT /id="PRO_0000076651"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 209..211
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 441
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 507
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 510
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 545
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 703
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 784..785
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 130
FT /note="H -> Y (in Ref. 1; CAA58046)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..233
FT /note="AT -> RP (in Ref. 1; CAA58046)"
FT /evidence="ECO:0000305"
FT CONFLICT 715..727
FT /note="SRRGNDEIMARGT -> VAVVMMRLWREH (in Ref. 1; CAA58046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 898 AA; 98152 MW; D90457C4FB0B56B8 CRC64;
MASENPFRSI LKALEKPDGG EFGNYYSLPA LNDPRIDKLP YSIRILLESA IRNCDEFQVK
SKDVEKILDW ENTSPKQVEI PFKPARVLLQ DFTGVPAVVD LACMRDAMNN LGGDSNKINP
LVPVDLVIDH SVQVDVARSE NAVQANMELE FQRNKERFAF LKWGSNAFHN MLVVPPGSGI
VHQVNLEYLA RVVFNTNGLL YPDSVVGTDS HTTMIDGLGV AGWGVGGIEA EATMLGQPMS
MVLPGVVGFK LTGKLRDGMT ATDLVLTVTQ MLRKHGVVGK FVEFHGEGMR ELSLADRATI
ANMSPEYGAT MGFFPVDHVT LQYLRLTGRS DDTVSMIEAY LRANKMFVDY SEPESKTVYS
SCLELNLEDV EPCVSGPKRP HDRVPLKEMK ADWHSCLDNR VGFKGFAVPK EAQSKAVEFN
FNGTTAQLRH GDVVIAAITS CTNTSNPSVM LGAALVAKKA CDLGLEVKPW IKTSLAPGSG
VVTKYLAKSG LQKYLNQLGF SIVGYGCTTC IGNSGDIHEA VASAIVDNDL VASAVLSGNR
NFEGRVHPLT RANYLASPPL VVAYALAGTV DIDFETQPIG TGKDGKQIFF RDIWPSNKEV
AEVVQSSVLP DMFKATYEAI TKGNSMWNQL SVASGTLYEW DPKSTYIHEP PYFKGMTMSP
PGPHGVKDAY CLLNFGDSIT TDHISPAGSI HKDSPAAKYL MERGVDRRDF NSYGSRRGND
EIMARGTFAN IRIVNKHLKG EVGPKTVHIP TGEKLSVFDA AMKYRNEGRD TIILAGAEYG
SGSSRDWAAK GPMLLGVKAV ISKSFERIHR SNLVGMGIIP LCFKAGEDAE TLGLTGQELY
TIELPNNVSE IKPGQDVTVV TNNGKSFTCT LRFDTEVELA YFDHGGILQY VIRNLIKQ
