Q94A28 (ACO3M_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aconitate hydratase 3, mitochondrial
Short name=Aconitase 3
EC=4.2.1.3

Alternative name(s):
Citrate hydro-lyase 3

Gene names

Name:	ACO3
Ordered Locus Names:	At4g26970
ORF Names:	F10M23.310

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	995 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity.
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	Mitochondrion Ref.4.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.
Sequence caution	The sequence CAB36543.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79552.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	citrate metabolic process Inferred from mutant phenotype. Source: TAIR glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW isocitrate metabolic process Inferred from mutant phenotype. Source: TAIR response to cadmium ion Inferred from expression pattern. Source: TAIR response to oxidative stress Inferred from mutant phenotype. Source: TAIR tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from direct assay. Source: TAIR cytosol Non-traceable author statement. Source: TAIR mitochondrion Inferred from direct assay Ref.4. Source: TAIR
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from mutant phenotype. Source: TAIR citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from direct assay. Source: TAIR isocitrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 83	83	Mitochondrion Potential
	Chain	84 – 995	912	Aconitate hydratase 3, mitochondrial		PRO_0000259922
Regions
	Region	306 – 308	3	Substrate binding By similarity
	Region	881 – 882	2	Substrate binding By similarity
Sites
	Metal binding	538	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	604	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	607	1	Iron-sulfur (4Fe-4S) By similarity
	Binding site	187	1	Substrate By similarity
	Binding site	637	1	Substrate By similarity
	Binding site	642	1	Substrate By similarity
	Binding site	800	1	Substrate By similarity
Experimental info
	Sequence conflict	407	1	T → A in AAK91447. Ref.3
	Sequence conflict	407	1	T → A in AAN18061. Ref.3
	Sequence conflict	463	1	D → E in CAB36543. Ref.1
	Sequence conflict	463	1	D → E in CAB79552. Ref.1
	Sequence conflict	903	1	E → G in AAK91447. Ref.3
	Sequence conflict	903	1	E → G in AAN18061. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q94A28 [UniParc]. Last modified May 3, 2011. Version 3. Checksum: 20FC18030F1CBDDB	FASTA	995	108,481
	10 20 30 40 50 60 MYRRATSGVR SASARLSSSL SRIASSETAS VSAPSASSLR NQTNRSKSFS SALRSFRVCS 70 80 90 100 110 120 ASTRWSHGGS WGSPASLRAQ ARNSTPVMEK FERKYATMAS EHSYKDILTS LPKPGGGEYG 130 140 150 160 170 180 KYYSLPALND PRIDKLPFSV RILLESAIRN CDNYQVTKDD VEKILDWENT STKQVEIAFK 190 200 210 220 230 240 PARVILQDFT GVPVLVDLAS MRDAVKNLGS DPSKINPLVP VDLVVDHSIQ VDFARSEDAA 250 260 270 280 290 300 QKNLELEFKR NKERFTFLKW GSTAFQNMLV VPPGSGIVHQ VNLEYLGRVV FNSKGFLYPD 310 320 330 340 350 360 SVVGTDSHTT MIDGLGVAGW GVGGIEAEAA MLGQPMSMVL PGVVGFKLDG KLKEGVTATD 370 380 390 400 410 420 LVLTVTQILR KHGVVGKFVE FYGEGMSELS LADRATIANM SPEYGATMGF FPVDHVTLEY 430 440 450 460 470 480 LKLTGRSDET VSMIESYLRA NNMFVDYNEP QQERAYTSYL QLDLGHVEPC ISGPKRPHDR 490 500 510 520 530 540 VPLKDMKADW HACLDNPVGF KGFAVPKEKQ EEVVKFSYNG QPAEIKHGSV VIAAITSCTN 550 560 570 580 590 600 TSNPSVMIGA ALVAKKASDL GLKVKPWVKT SLAPGSRVVE KYLDRSGLRE SLTKQGFEIV 610 620 630 640 650 660 GYGCTTCIGN SGNLDPEVAS AIEGTDIIPA AVLSGNRNFE GRVHPQTRAN YLASPPLVVA 670 680 690 700 710 720 YALAGTVDID FEKEPIGTRS DGKSVYLRDV WPSNEEVAQV VQYSVLPSMF KSSYETITEG 730 740 750 760 770 780 NPLWNELSAP SSTLYSWDPN STYIHEPPYF KNMTANPPGP REVKDAYCLL NFGDSVTTDH 790 800 810 820 830 840 ISPAGNIQKT SPAAKFLMDR GVISEDFNSY GSRRGNDEVM ARGTFANIRI VNKLLKGEVG 850 860 870 880 890 900 PNTVHIPTGE KLSVFDAASK YKTAEQDTII LAGAEYGSGS SRDWAAKGPL LLGVKAVIAK 910 920 930 940 950 960 SFERIHRSNL AGMGIIPLCF KAGEDAETLG LTGHERYTVH LPTKVSDIRP GQDVTVTTDS 970 980 990 GKSFVCTLRF DTEVELAYYD HGGILPYVIR SLSAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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]	"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]. Strain: cv. Landsberg erecta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL035440 Genomic DNA. Translation: CAB36543.1. Sequence problems. AL161566 Genomic DNA. Translation: CAB79552.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE85279.1. AY050431 mRNA. Translation: AAK91447.1. BT000492 mRNA. Translation: AAN18061.1.
IPI	IPI00528274.
PIR	T04820.
RefSeq	NP_567763.2. NM_118831.4.
UniGene	At.22696. At.48905.
3D structure databases
HSSP	HSSP built from PDB template 2B3Y based on UniProtKB P21399.
ProteinModelPortal	Q94A28.
SMR	Q94A28. Positions 121-993.
ModBase	Search...
Protein-protein interaction databases
STRING	Q94A28.
Proteomic databases
PRIDE	Q94A28.
ProMEX	Q94A28.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G26970.1; AT4G26970.1; AT4G26970.
GeneID	828805.
GenomeReviews	Gene locus AT4G26970 in contig CT486007_GR.
KEGG	ath:AT4G26970.
NMPDR	fig|3702.1.peg.20630.
Organism-specific databases
GeneFarm	43006. 434.
TAIR	At4g26970.
Phylogenomic databases
GeneTree	EPGT00070000028605.
HOGENOM	HBG289738.
InParanoid	Q94A28.
Gene expression databases
Genevestigator	Q94A28.
Family and domain databases
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. 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. 3 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
KO	K01681.
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.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF53732. Aconitase_N. 1 hit.
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

ACO3M_ARATH

Accession

Primary (citable) accession number: Q94A28
Secondary accession number(s): Q9SZ36

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	May 3, 2011
Last modified:	December 14, 2011
This is version 69 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program