P19414 · ACON_YEAST
- ProteinAconitate hydratase, mitochondrial
- GeneACO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids778 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Can also provide minor contributions to the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. Also plays an essential role in mtDNA maintenance. May directly protect mtDNA from accumulation of point mutations and ssDNA breaks as a component of mitochondrial nucleoids, or by preventing accumulation of iron citrate thereby alleviating its detrimental effects in mitochondria.
Miscellaneous
The fermenting yeast S.cerevisiae has 2 aconitases, ACO1 essential for the citric acid cycle, and ACO2 specifically and exclusively contributing to lysine biosynthesis. In contrast, in respiring filamentous fungi the ACO2 homologs (acoB) seem enzymatically inactive and the ACO1 homolog (acoA) is solely responsible for these functions.
Present with 96700 molecules/cell in log phase SD medium.
Catalytic activity
- citrate = D-threo-isocitrate
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit.
Activity regulation
Subject to catabolite regulation.
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 | 95 | substrate | ||||
Sequence: Q | ||||||
Binding site | 188-190 | substrate | ||||
Sequence: DSH | ||||||
Binding site | 382 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 445 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 448 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 471 | substrate | ||||
Sequence: R | ||||||
Binding site | 476 | substrate | ||||
Sequence: R | ||||||
Binding site | 604 | substrate | ||||
Sequence: R | ||||||
Binding site | 667-668 | substrate | ||||
Sequence: SR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrial nucleoid | |
Cellular Component | mitochondrion | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | aconitate hydratase activity | |
Molecular Function | double-stranded DNA binding | |
Molecular Function | iron-sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA binding | |
Molecular Function | single-stranded DNA binding | |
Biological Process | mitochondrial genome maintenance | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAconitate hydratase, mitochondrial
- EC number
- Short namesAconitase
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP19414
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Mainly mitochondrial, small amounts are also detected in the cytosol with a ratio of 94:6.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Essential for growth on nonfermentable carbon sources and for biosynthesis of glutamate. Causes a dramatic increase in cellular citrate levels.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 604 | Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate. | ||||
Sequence: R → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 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 | 1-16 | Mitochondrion | ||||
Sequence: MLSARSAIKRPIVRGL | ||||||
Chain | PRO_0000000547 | 17-778 | Aconitate hydratase, mitochondrial | |||
Sequence: ATVSNLTRDSKVNQNLLEDHSFINYKQNVETLDIVRKRLNRPFTYAEKILYGHLDDPHGQDIQRGVSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPVTVHCDHLIQAQVGGEKDLKRAIDLNKEVYDFLASATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGKIADFAKLYHKDLLSADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVANNWPLDVRVGLIGSCTNSSYEDMSRSASIVKDAAAHGLKSKTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQWDRRDIKKGDKNTIVSSYNRNFTSRNDGNPQTHAFVASPELVTAFAIAGDLRFNPLTDKLKDKDGNEFMLKPPHGDGLPQRGYDAGENTYQAPPADRSTVEVKVSPTSDRLQLLKPFKPWDGKDAKDMPILIKAVGKTTTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKNVYTGEYKGVPDTARDYRDQGIKWVVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDKINPDDRIDILGLAELAPGKPVTMRVHPKNGKPWDAVLTHTFNDEQIEWFKYGSALNKIKADEKK | ||||||
Modified residue | 391 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 409 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 556 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Highly induced in the absence of glutamate. Induction is further increased when both glutamate and lysine are missing.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length778
- Mass (Da)85,368
- Last updated1995-11-01 v2
- ChecksumAA9EB9A24388090E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 527-549 | in Ref. 1; AAA34389 | ||||
Sequence: DGLPQRGYDAGENTYQAPPADRS → RWFASKEVMMLVRTLTKLHLQTVA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M33131 EMBL· GenBank· DDBJ | AAA34389.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U17243 EMBL· GenBank· DDBJ | AAB67348.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09613.1 EMBL· GenBank· DDBJ | Genomic DNA |