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Q9SIB9 (ACO2M_ARATH) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length990 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcitrate 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_componentcell 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 11743115PubMed 12492832Ref.4PubMed 17137349PubMed 18385124. Source: TAIR

vacuolar membrane

Inferred from direct assay PubMed 17151019. Source: TAIR

   Molecular_function4 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7878Mitochondrion Potential
Chain79 – 990912Aconitate hydratase 2, mitochondrial
PRO_0000259921

Regions

Region301 – 3033Substrate binding By similarity
Region876 – 8772Substrate binding By similarity

Sites

Metal binding5331Iron-sulfur (4Fe-4S) By similarity
Metal binding5991Iron-sulfur (4Fe-4S) By similarity
Metal binding6021Iron-sulfur (4Fe-4S) By similarity
Binding site1821Substrate By similarity
Binding site6321Substrate By similarity
Binding site6371Substrate By similarity
Binding site7951Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SIB9 [UniParc].

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

FASTA990108,201
        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' 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. expand/collapse author list , 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] [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. expand/collapse author list , 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] [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.
IPIIPI00543590.
PIRB84471.
RefSeqNP_178634.2. NM_126589.2.
UniGeneAt.26759.
At.67769.

3D structure databases

HSSPHSSP built from PDB template 2B3Y based on UniProtKB P21399.
ProteinModelPortalQ9SIB9.
SMRQ9SIB9. Positions 116-989.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9SIB9. 1 interaction.

Proteomic databases

PaxDbQ9SIB9.
PRIDEQ9SIB9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G05710.1; AT2G05710.1; AT2G05710.
GeneID815120.
KEGGath:AT2G05710.

Organism-specific databases

GeneFarm4276. 434.
TAIRAt2g05710.

Phylogenomic databases

eggNOGCOG1048.
HOGENOMHOG000025704.
InParanoidQ9SIB9.
KOK01681.
OMADEALYKW.
PhylomeDBQ9SIB9.
ProtClustDBPLN00070.

Enzyme and pathway databases

UniPathwayUPA00223; UER00718.

Gene expression databases

ArrayExpressQ9SIB9.
GenevestigatorQ9SIB9.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
InterProIPR015931. 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]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF1. PTHR11670:SF1. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR01341. aconitase_1. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACO2M_ARATH
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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