Aconitate hydratase 2, mitochondrial precursor - Arabidopsis thaliana (Mouse-ear cress)

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Q9SIB9 (ACO2M_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome]

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	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)

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.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.
Sequence caution	The sequence AAD25640.1 differs from that shown. Reason: Erroneous initiation.

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 PubMed 17013749. Source: TAIR glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW isocitrate metabolic process Inferred from mutant phenotype PubMed 17013749. Source: TAIR response to abscisic acid stimulus Inferred from expression pattern PubMed 18768909. Source: TAIR response to cadmium ion Inferred from expression pattern PubMed 16502469. Source: TAIR response to oxidative stress Inferred from direct assay PubMed 12492832. Source: TAIR response to salt stress Inferred from expression pattern PubMed 17916636. Source: TAIR tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cell wall Inferred from direct assay PubMed 16287169. Source: TAIR chloroplast stroma Inferred from direct assay PubMed 20061580. Source: TAIR cytosol Non-traceable author statement PubMed 17013749. Source: TAIR mitochondrion Inferred from direct assay PubMed 11743115 PubMed 12492832 Ref.4 PubMed 17137349 PubMed 18385124. Source: TAIR vacuolar membrane Inferred from direct assay PubMed 17151019. Source: TAIR
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW ATP binding Inferred from direct assay PubMed 17137349. Source: TAIR aconitate hydratase activity Inferred from mutant phenotype PubMed 17013749. Source: TAIR citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from direct assay PubMed 20018591. 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 – 78

Mitochondrion Potential

Chain

79 – 990

912

Aconitate hydratase 2, mitochondrial

PRO_0000259921

Regions

Region

301 – 303

Substrate binding By similarity

Region

876 – 877

Substrate binding By similarity

Sites

Metal binding

533

Iron-sulfur (4Fe-4S) By similarity

Metal binding

599

Iron-sulfur (4Fe-4S) By similarity

Metal binding

602

Iron-sulfur (4Fe-4S) By similarity

Binding site

182

Substrate By similarity

Binding site

632

Substrate By similarity

Binding site

637

Substrate By similarity

Binding site

795

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9SIB9 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: 552AE563BC2981ED
Show »

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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' 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. Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [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] [Europe PMC] [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	AC007170 Genomic DNA. Translation: AAD25640.1. Different initiation. CP002685 Genomic DNA. Translation: AEC05964.1. AY136414 mRNA. Translation: AAM97080.1. BT008809 mRNA. Translation: AAP68248.1.
IPI	IPI00543590.
PIR	B84471.
RefSeq	NP_178634.2. NM_126589.2.
UniGene	At.26759. At.67769.
3D structure databases
HSSP	HSSP built from PDB template 2B3Y based on UniProtKB P21399.
ProteinModelPortal	Q9SIB9.
SMR	Q9SIB9. Positions 116-989.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SIB9. 1 interaction.
Proteomic databases
PaxDb	Q9SIB9.
PRIDE	Q9SIB9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G05710.1; AT2G05710.1; AT2G05710.
GeneID	815120.
KEGG	ath:AT2G05710.
Organism-specific databases
GeneFarm	4276. 434.
TAIR	At2g05710.
Phylogenomic databases
eggNOG	COG1048.
HOGENOM	HOG000025704.
InParanoid	Q9SIB9.
KO	K01681.
OMA	DEALYKW.
PhylomeDB	Q9SIB9.
ProtClustDB	PLN00070.
Enzyme and pathway databases
UniPathway	UPA00223; UER00718.
Gene expression databases
ArrayExpress	Q9SIB9.
Genevestigator	Q9SIB9.
Family and domain databases
Gene3D	3.20.19.10. 1 hit. 3.30.499.10. 3 hits. 3.40.1060.10. 1 hit.
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]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF1. PTHR11670:SF1. 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

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:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents