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   16-JUN-2009, entry version 83.
DE   RecName: Full=Aconitate hydratase 1;
DE            Short=Aconitase 1;
DE            EC=4.2.1.3;
DE   AltName: Full=Citrate hydro-lyase 1;
GN   Name=ACO1; Synonyms=ACO; OrderedLocusNames=At4g35830;
GN   ORFNames=F4B14.100;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=95229629; 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
RT   with 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   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 44-52 AND 472-485.
RC   TISSUE=Leaf, and Stem;
RX   MEDLINE=21608403; PubMed=11743114; DOI=10.1104/pp.127.4.1694;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
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
RT   highlights signaling and regulatory components, provides assessment of
RT   targeting prediction programs, and indicates plant-specific
RT   mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
CC   -!- CATALYTIC ACTIVITY: Citrate = isocitrate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
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   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
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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; AY062772; AAL32850.1; -; mRNA.
DR   IPI; IPI00530419; -.
DR   PIR; T04693; T04693.
DR   RefSeq; NP_195308.1; -.
DR   UniGene; At.24717; -.
DR   HSSP; P20004; 1AMJ.
DR   PRIDE; Q42560; -.
DR   GeneID; 829737; -.
DR   GenomeReviews; CT486007_GR; AT4G35830.
DR   NMPDR; fig|3702.1.peg.21674; -.
DR   GeneFarm; 4280; 434.
DR   TAIR; At4g35830; -.
DR   OMA; Q42560; VPKTSTE.
DR   BRENDA; 4.2.1.3; 302.
DR   ArrayExpress; Q42560; -.
DR   GermOnline; AT4G35830; Arabidopsis thaliana.
DR   GO; GO:0048046; C:apoplast; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015937; Aconitase-like_core.
DR   InterPro; IPR006249; Aconitase/Fe_reg_prot_2.
DR   InterPro; IPR015934; Aconitase/Fe_reg_prot_2/AcnD.
DR   InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   Gene3D; G3DSA:3.30.499.10; Acnase/IPM_dHydase_lsu_aba_1/3; 2.
DR   Gene3D; G3DSA:3.40.1060.10; Aconitase/IPMdHydase_lsu_aba_2; 1.
DR   PANTHER; PTHR11670; Aconitase-like_core; 1.
DR   PANTHER; PTHR11670:SF1; Aconitase/Fe_reg_prot_2/AcnD; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   ProDom; PD000511; Aconitase_N; 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; Alternative splicing; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   Mitochondrion; Tricarboxylic acid cycle.
FT   CHAIN         1    898       Aconitate hydratase 1.
FT                                /FTId=PRO_0000076651.
FT   METAL       441    441       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       507    507       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       510    510       Iron-sulfur (4Fe-4S) (By similarity).
FT   CONFLICT    130    130       H -> Y (in Ref. 1; CAA58046).
FT   CONFLICT    232    233       AT -> RP (in Ref. 1; CAA58046).
FT   CONFLICT    715    727       SRRGNDEIMARGT -> VAVVMMRLWREH (in Ref.
FT                                1).
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
//