Reviewed, UniProtKB/Swiss-Prot Q9SIB9 (ACO2M_ARATH)

Names and origin

Protein names

Recommended name:
    Aconitate hydratase 2, mitochondrial
      Short name=Aconitase 2
    EC=4.2.1.3
Alternative name(s):
    Citrate hydro-lyase 2

Gene names

Name:	ACO2
Ordered Locus Names:	At2g05710
ORF Names:	T3P4.5

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	990 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)

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.3.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

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
Gene Ontology (GO)
Biological process	glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW response to abscisic acid stimulus Inferred from expression pattern. Source: TAIR response to cadmium ion Inferred from expression pattern. Source: TAIR response to oxidative stress Inferred from direct assay. Source: TAIR response to salt stress Inferred from expression pattern. Source: TAIR tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from direct assay. Source: TAIR chloroplast Inferred from direct assay. Source: TAIR mitochondrion Ref.3 Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW ATP binding Inferred from direct assay. Source: TAIR aconitate hydratase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 78	78	Mitochondrion Potential
	Chain	79 – 990	912	Aconitate hydratase 2, mitochondrial		PRO_0000259921
Sites
	Metal binding	533	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	599	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	602	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9SIB9-1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 552AE563BC2981ED	FASTA	990	108,201
	10 20 30 40 50 60 MYLTASSSAS SSIIRAASSR SSSLFSFRSV LSPSVSSTSP SSLLARRSFG TISPAFRRWS 70 80 90 100 110 120 HSFHSKPSPF RFTSQIRAVS PVLDRLQRTF SSMASEHPFK GIFTTLPKPG GGEFGKFYSL 130 140 150 160 170 180 PALNDPRVDK LPYSIRILLE SAIRNCDNFQ VTKEDVEKII DWEKTSPKQV EIPFKPARVL 190 200 210 220 230 240 LQDFTGVPAV VDLACMRDAM NKLGSDSNKI NPLVPVDLVI DHSVQVDVAR SENAVQANME 250 260 270 280 290 300 LEFQRNKERF AFLKWGSTAF QNMLVVPPGS GIVHQVNLEY LGRVVFNTKG LLYPDSVVGT 310 320 330 340 350 360 DSHTTMIDGL GVAGWGVGGI EAEATMLGQP MSMVLPGVVG FKLAGKMRNG VTATDLVLTV 370 380 390 400 410 420 TQMLRKHGVV GKFVEFYGNG MSGLSLADRA TIANMSPEYG ATMGFFPVDH VTLQYLKLTG 430 440 450 460 470 480 RSDETVAMIE AYLRANNMFV DYNEPQQDRV YSSYLELNLD DVEPCISGPK RPHDRVTLKE 490 500 510 520 530 540 MKADWHSCLD SKVGFKGFAI PKEAQEKVVN FSFDGQPAEL KHGSVVIAAI TSCTNTSNPS 550 560 570 580 590 600 VMLGAGLVAK KACDLGLQVK PWIKTSLAPG SGVVTKYLLK SGLQEYLNEQ GFNIVGYGCT 610 620 630 640 650 660 TCIGNSGEIN ESVGAAITEN DIVAAAVLSG NRNFEGRVHP LTRANYLASP PLVVAYALAG 670 680 690 700 710 720 TVNIDFETEP IGKGKNGKDV FLRDIWPTTE EIAEVVQSSV LPDMFRATYE SITKGNPMWN 730 740 750 760 770 780 KLSVPENTLY SWDPNSTYIH EPPYFKDMTM DPPGPHNVKD AYCLLNFGDS ITTDHISPAG 790 800 810 820 830 840 NIQKDSPAAK FLMERGVDRK DFNSYGSRRG NDEIMARGTF ANIRIVNKLM NGEVGPKTVH 850 860 870 880 890 900 IPSGEKLSVF DAAMRYKSSG EDTIILAGAE YGSGSSRDWA AKGPMLQGVK AVIAKSFERI 910 920 930 940 950 960 HRSNLVGMGI IPLCFKSGED ADTLGLTGHE RYTIHLPTDI SEIRPGQDVT VTTDNGKSFT 970 980 990 CTVRFDTEVE LAYFNHGGIL PYVIRNLSKQ

References

[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	"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	AC007170 Genomic DNA. Translation: AAD25640.1. Different initiation. AY136414 mRNA. Translation: AAM97080.1. BT008809 mRNA. Translation: AAP68248.1.
IPI	IPI00543590.
PIR	B84471.
RefSeq	NP_178634.2.
UniGene	At.26759 At.67769 Rra.22920 Rra.2838 Rsa.2580
3D structure databases
HSSP	HSSP built from PDB template 2B3Y based on UniProtKB P21399.
SMR	Q9SIB9. Positions 116-989.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SIB9.
2-D gel databases
ANU-2DPAGE	Q9SIB9.
Proteomic databases
PRIDE	Q9SIB9.
Genome annotation databases
GeneID	815120.
GenomeReviews	Gene locus AT2G05710 in contig CT485783_GR.
KEGG	ath:AT2G05710.
NMPDR	fig|3702.1.peg.8129.
Organism-specific databases
GeneFarm	4276. 434.
TAIR	At2g05710.
Phylogenomic databases
HOGENOM	HBG289738.
InParanoid	Q9SIB9.
OMA	MLYPDSV.
PhylomeDB	Q9SIB9.
Enzyme and pathway databases
BRENDA	4.2.1.3. 302.
Gene expression databases
Genevestigator	Q9SIB9.
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

ACO2M_ARATH

Accession

Primary (citable) accession number: Q9SIB9
Secondary accession number(s): Q8L784

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 28, 2006
Last modified:	February 9, 2010
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)