Q9SIB9 · ACO3M_ARATH
- ProteinAconitate hydratase 3, mitochondrial
- GeneACO3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids990 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. Contributes to oxidative stress tolerance (PubMed:17013749).
Modulates cytosolic citrate metabolism during lipid mobilization. Required during seedling growth (PubMed:25061985).
Modulates cytosolic citrate metabolism during lipid mobilization. Required during seedling growth (PubMed:25061985).
Catalytic activity
- citrate = D-threo-isocitrate
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit.
Pathway
Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 182 | substrate | ||||
Sequence: Q | ||||||
Binding site | 301-303 | substrate | ||||
Sequence: DSH | ||||||
Binding site | 533 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 599 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 602 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 632 | substrate | ||||
Sequence: R | ||||||
Binding site | 637 | substrate | ||||
Sequence: R | ||||||
Binding site | 795 | substrate | ||||
Sequence: R | ||||||
Binding site | 876-877 | substrate | ||||
Sequence: SR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast stroma | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Cellular Component | plant-type cell wall | |
Cellular Component | plant-type vacuole | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | aconitate hydratase activity | |
Molecular Function | ATP binding | |
Molecular Function | copper ion binding | |
Biological Process | citrate metabolic process | |
Biological Process | glyoxylate cycle | |
Biological Process | isocitrate metabolic process | |
Biological Process | response to abscisic acid | |
Biological Process | response to oxidative stress | |
Biological Process | seedling development | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAconitate hydratase 3, mitochondrial
- EC number
- Short namesAconitase 3 ; mACO1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9SIB9
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Cytosolic localization in 3-day-old seedlings, but mitochondrial in 10-day-old plantlets.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Reduced cytosolic and mitochondrial aconitase (ACO) activities by 25 and 55 precent, respectively (PubMed:17013749, PubMed:17437406).
Increased tolerance to oxidative stress mediated by paraquat, a superoxide-generating agent (PubMed:17013749).
Delayed early seedling growth, altered assimilation of acetate feeding and elevated citrate and malate levels (PubMed:25061985).
Increased tolerance to oxidative stress mediated by paraquat, a superoxide-generating agent (PubMed:17013749).
Delayed early seedling growth, altered assimilation of acetate feeding and elevated citrate and malate levels (PubMed:25061985).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 57 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-78 | Mitochondrion | ||||
Sequence: MYLTASSSASSSIIRAASSRSSSLFSFRSVLSPSVSSTSPSSLLARRSFGTISPAFRRWSHSFHSKPSPFRFTSQIRA | ||||||
Chain | PRO_0000259921 | 79-990 | Aconitate hydratase 3, mitochondrial | |||
Sequence: VSPVLDRLQRTFSSMASEHPFKGIFTTLPKPGGGEFGKFYSLPALNDPRVDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWEKTSPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTKGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIEAYLRANNMFVDYNEPQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEMKADWHSCLDSKVGFKGFAIPKEAQEKVVNFSFDGQPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKTSLAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGAAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVNIDFETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQSSVLPDMFRATYESITKGNPMWNKLSVPENTLYSWDPNSTYIHEPPYFKDMTMDPPGPHNVKDAYCLLNFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIHLPTDISEIRPGQDVTVTTDNGKSFTCTVRFDTEVELAYFNHGGILPYVIRNLSKQ | ||||||
Modified residue | 91 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated at Ser-91 in the cytoplasm; this phosphorylation requires the presence of B'GAMMA.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length990
- Mass (Da)108,201
- Last updated2006-11-28 v2
- Checksum552AE563BC2981ED
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC007170 EMBL· GenBank· DDBJ | AAD25640.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
CP002685 EMBL· GenBank· DDBJ | AEC05964.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY136414 EMBL· GenBank· DDBJ | AAM97080.1 EMBL· GenBank· DDBJ | mRNA | ||
BT008809 EMBL· GenBank· DDBJ | AAP68248.1 EMBL· GenBank· DDBJ | mRNA |