Reviewed, UniProtKB/Swiss-Prot Q42560 (ACO1_ARATH)

Names and origin

Protein names

Recommended name:
    Aconitate hydratase 1
      Short name=Aconitase 1
    EC=4.2.1.3
Alternative name(s):
    Citrate hydro-lyase 1

Gene names

Name:	ACO1
Synonyms:	ACO
Ordered Locus Names:	At4g35830
ORF Names:	F4B14.100

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	898 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Citrate = isocitrate.
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. Mitochondrion Ref.5.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative splicing
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	response to salt stress Inferred from expression pattern. Source: TAIR tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apoplast Inferred from direct assay. Source: TAIR mitochondrion Ref.5 Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q42560-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 898	898	Aconitate hydratase 1		PRO_0000076651
Sites
	Metal binding	441	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	507	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	510	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	130	1	H → Y in CAA58046. Ref.1
	Sequence conflict	232 – 233	2	AT → RP in CAA58046. Ref.1
	Sequence conflict	715 – 727	13	SRRGN…MARGT → VAVVMMRLWREH Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: D90457C4FB0B56B8	FASTA	898	98,152
	10 20 30 40 50 60 MASENPFRSI LKALEKPDGG EFGNYYSLPA LNDPRIDKLP YSIRILLESA IRNCDEFQVK 70 80 90 100 110 120 SKDVEKILDW ENTSPKQVEI PFKPARVLLQ DFTGVPAVVD LACMRDAMNN LGGDSNKINP 130 140 150 160 170 180 LVPVDLVIDH SVQVDVARSE NAVQANMELE FQRNKERFAF LKWGSNAFHN MLVVPPGSGI 190 200 210 220 230 240 VHQVNLEYLA RVVFNTNGLL YPDSVVGTDS HTTMIDGLGV AGWGVGGIEA EATMLGQPMS 250 260 270 280 290 300 MVLPGVVGFK LTGKLRDGMT ATDLVLTVTQ MLRKHGVVGK FVEFHGEGMR ELSLADRATI 310 320 330 340 350 360 ANMSPEYGAT MGFFPVDHVT LQYLRLTGRS DDTVSMIEAY LRANKMFVDY SEPESKTVYS 370 380 390 400 410 420 SCLELNLEDV EPCVSGPKRP HDRVPLKEMK ADWHSCLDNR VGFKGFAVPK EAQSKAVEFN 430 440 450 460 470 480 FNGTTAQLRH GDVVIAAITS CTNTSNPSVM LGAALVAKKA CDLGLEVKPW IKTSLAPGSG 490 500 510 520 530 540 VVTKYLAKSG LQKYLNQLGF SIVGYGCTTC IGNSGDIHEA VASAIVDNDL VASAVLSGNR 550 560 570 580 590 600 NFEGRVHPLT RANYLASPPL VVAYALAGTV DIDFETQPIG TGKDGKQIFF RDIWPSNKEV 610 620 630 640 650 660 AEVVQSSVLP DMFKATYEAI TKGNSMWNQL SVASGTLYEW DPKSTYIHEP PYFKGMTMSP 670 680 690 700 710 720 PGPHGVKDAY CLLNFGDSIT TDHISPAGSI HKDSPAAKYL MERGVDRRDF NSYGSRRGND 730 740 750 760 770 780 EIMARGTFAN IRIVNKHLKG EVGPKTVHIP TGEKLSVFDA AMKYRNEGRD TIILAGAEYG 790 800 810 820 830 840 SGSSRDWAAK GPMLLGVKAV ISKSFERIHR SNLVGMGIIP LCFKAGEDAE TLGLTGQELY 850 860 870 880 890 TIELPNNVSE IKPGQDVTVV TNNGKSFTCT LRFDTEVELA YFDHGGILQY VIRNLIKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure, genomic organization, and expression of the Arabidopsis thaliana aconitase gene. Plant aconitase show significant homology with mammalian iron-responsive element-binding protein." Peyret P., Perez P., Alric M. J. Biol. Chem. 270:8131-8137(1995) [PubMed: 7713917] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Proteomic approach to identify novel mitochondrial proteins in Arabidopsis." Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P. Plant Physiol. 127:1694-1710(2001) [PubMed: 11743114] [Abstract] Cited for: PROTEIN SEQUENCE OF 44-52 AND 472-485. Tissue: Leaf and Stem.
[5]	"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed: 14671022] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X82839 mRNA. Translation: CAA58046.1. Different initiation. AL031986 Genomic DNA. Translation: CAA21469.1. AL161588 Genomic DNA. Translation: CAB81492.1. AY062772 mRNA. Translation: AAL32850.1.
IPI	IPI00530419.
PIR	T04693.
RefSeq	NP_195308.1.
UniGene	At.24717 Rra.16718 Rsa.4710
3D structure databases
SMR	Q42560. Positions 5-897.
ModBase	Search...
Protein-protein interaction databases
STRING	Q42560.
Proteomic databases
PRIDE	Q42560.
Genome annotation databases
GeneID	829737.
GenomeReviews	Gene locus AT4G35830 in contig CT486007_GR.
NMPDR	fig|3702.1.peg.21674.
Organism-specific databases
GeneFarm	4280. 434.
TAIR	At4g35830.
Phylogenomic databases
HOGENOM	HBG289738.
InParanoid	Q42560.
OMA	NIASNSP.
PhylomeDB	Q42560.
Enzyme and pathway databases
BRENDA	4.2.1.3. 302.
Gene expression databases
ArrayExpress	Q42560.
Genevestigator	Q42560.
GermOnline	AT4G35830. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR006249. Aconitase/Fe_reg_prot_2. IPR015934. Aconitase/Fe_reg_prot_2/AcnD. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
TIGRFAMs	TIGR01341. aconitase_1. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACO1_ARATH

Accession

Primary (citable) accession number: Q42560
Secondary accession number(s): Q9SZT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 21, 2001
Last modified:	February 9, 2010
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)