Q99798 · ACON_HUMAN
- ProteinAconitate hydratase, mitochondrial
- GeneACO2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids780 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
Catalytic activity
- citrate = D-threo-isocitrate
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme.
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 | 99 | substrate | ||||
Sequence: Q | ||||||
Binding site | 192-194 | substrate | ||||
Sequence: DSH | ||||||
Binding site | 385 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 448 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 451 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 474 | substrate | ||||
Sequence: R | ||||||
Binding site | 479 | substrate | ||||
Sequence: R | ||||||
Binding site | 607 | substrate | ||||
Sequence: R | ||||||
Binding site | 670-671 | substrate | ||||
Sequence: SR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | 3 iron, 4 sulfur cluster binding | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | aconitate hydratase activity | |
Molecular Function | iron ion binding | |
Biological Process | citrate metabolic process | |
Biological Process | generation of precursor metabolites and energy | |
Biological Process | isocitrate metabolic process | |
Biological Process | liver development | |
Biological Process | response to isolation stress | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAconitate hydratase, mitochondrial
- EC number
- Short namesAconitase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ99798
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Infantile cerebellar-retinal degeneration (ICRD)
- Note
- DescriptionA severe autosomal recessive neurodegenerative disorder characterized by onset between ages 2 and 6 months of truncal hypotonia, athetosis, seizures, and ophthalmologic abnormalities, particularly optic atrophy and retinal degeneration. Affected individuals show profound psychomotor retardation, with only some achieving rolling, sitting, or recognition of family. Brain MRI shows progressive cerebral and cerebellar degeneration.
- See alsoMIM:614559
Natural variants in ICRD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067543 | 112 | S>R | in ICRD; functional expression studies in yeast show that the mutant has decreased function under growth conditions requiring the TCA cycle and the glyoxylate shunt; dbSNP:rs786200924 | |
VAR_073436 | 259 | G>D | in ICRD; dbSNP:rs786204828 | |
VAR_073438 | 736 | K>N | in ICRD; dbSNP:rs786204829 |
Optic atrophy 9 (OPA9)
- Note
- DescriptionA condition that features progressive visual loss in association with optic atrophy. Atrophy of the optic disk indicates a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts.
- See alsoMIM:616289
Natural variants in OPA9
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_073435 | 74 | L>V | in OPA9; dbSNP:rs141772938 | |
VAR_073437 | 661 | G>R | in OPA9; dbSNP:rs752034900 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_073435 | 74 | in OPA9; dbSNP:rs141772938 | |||
Sequence: L → V | ||||||
Natural variant | VAR_067543 | 112 | in ICRD; functional expression studies in yeast show that the mutant has decreased function under growth conditions requiring the TCA cycle and the glyoxylate shunt; dbSNP:rs786200924 | |||
Sequence: S → R | ||||||
Natural variant | VAR_073436 | 259 | in ICRD; dbSNP:rs786204828 | |||
Sequence: G → D | ||||||
Natural variant | VAR_073437 | 661 | in OPA9; dbSNP:rs752034900 | |||
Sequence: G → R | ||||||
Natural variant | VAR_036572 | 697 | in a breast cancer sample; somatic mutation | |||
Sequence: T → N | ||||||
Natural variant | VAR_073438 | 736 | in ICRD; dbSNP:rs786204829 | |||
Sequence: K → N | ||||||
Natural variant | VAR_033297 | 768 | in dbSNP:rs1804785 | |||
Sequence: A → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 736 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-27 | UniProt | Mitochondrion | ||||
Sequence: MAPYSLLVTRLQKALGVRQYHVASVLC | |||||||
Chain | PRO_0000000541 | 28-780 | UniProt | Aconitate hydratase, mitochondrial | |||
Sequence: QRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLNRPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDYLTGTDGKKFRLEAPDADELPKGEFDPGQDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTPGKPLKCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ | |||||||
Modified residue | 31 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 50 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 50 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 138 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 138 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 144 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 144 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 233 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 233 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 411 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 549 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 552 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 559 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 559 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 573 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 573 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 577 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 591 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 605 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 605 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 628 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 670 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 689 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 723 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 723 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 730 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 730 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 736 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 739 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 743 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 528-560 | Disordered | ||||
Sequence: DADELPKGEFDPGQDTYQHPPKDSSGQHVDVSP | ||||||
Compositional bias | 545-560 | Polar residues | ||||
Sequence: QHPPKDSSGQHVDVSP |
Sequence similarities
Belongs to the aconitase/IPM isomerase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length780
- Mass (Da)85,425
- Last updated2000-05-30 v2
- Checksum58C9FFBDBDC63D5E
Computationally mapped potential isoform sequences
There are 16 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A2A274 | A2A274_HUMAN | ACO2 | 805 | ||
A0A7I2V2Y4 | A0A7I2V2Y4_HUMAN | ACO2 | 92 | ||
A0A7I2V3C8 | A0A7I2V3C8_HUMAN | ACO2 | 324 | ||
A0A7I2V3F1 | A0A7I2V3F1_HUMAN | ACO2 | 788 | ||
A0A7I2V3U0 | A0A7I2V3U0_HUMAN | ACO2 | 725 | ||
A0A7I2V3U7 | A0A7I2V3U7_HUMAN | ACO2 | 160 | ||
A0A7I2V499 | A0A7I2V499_HUMAN | ACO2 | 69 | ||
A0A7I2V4I8 | A0A7I2V4I8_HUMAN | ACO2 | 288 | ||
A0A7I2V538 | A0A7I2V538_HUMAN | ACO2 | 487 | ||
A0A7I2V586 | A0A7I2V586_HUMAN | ACO2 | 747 | ||
A0A7I2V5A1 | A0A7I2V5A1_HUMAN | ACO2 | 716 | ||
A0A7I2V614 | A0A7I2V614_HUMAN | ACO2 | 731 | ||
A0A7I2V5U4 | A0A7I2V5U4_HUMAN | ACO2 | 80 | ||
A0A7I2V5W7 | A0A7I2V5W7_HUMAN | ACO2 | 324 | ||
A0A7I2V5T4 | A0A7I2V5T4_HUMAN | ACO2 | 775 | ||
A0A7I2V6A6 | A0A7I2V6A6_HUMAN | ACO2 | 422 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 35 | in Ref. 1; AAB38416 | ||||
Sequence: S → T | ||||||
Sequence conflict | 136 | in Ref. 1; AAB38416 | ||||
Sequence: G → D | ||||||
Sequence conflict | 159 | in Ref. 1; AAB38416 | ||||
Sequence: A → D | ||||||
Sequence conflict | 167 | in Ref. 1; AAB38416 | ||||
Sequence: K → S | ||||||
Sequence conflict | 199 | in Ref. 4; CAG38805 | ||||
Sequence: G → D | ||||||
Sequence conflict | 207 | in Ref. 6; AAH26196 | ||||
Sequence: G → R | ||||||
Sequence conflict | 242 | in Ref. 1; AAB38416 | ||||
Sequence: S → T | ||||||
Sequence conflict | 270 | in Ref. 6; AAH26196 | ||||
Sequence: P → H | ||||||
Sequence conflict | 275 | in Ref. 1; AAB38416 | ||||
Sequence: I → M | ||||||
Sequence conflict | 444 | in Ref. 4; CAG38805 | ||||
Sequence: L → P | ||||||
Sequence conflict | 517 | in Ref. 1; AAB38416 | ||||
Sequence: T → K | ||||||
Compositional bias | 545-560 | Polar residues | ||||
Sequence: QHPPKDSSGQHVDVSP | ||||||
Sequence conflict | 553 | in Ref. 1; AAB38416 | ||||
Sequence: G → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U80040 EMBL· GenBank· DDBJ | AAB38416.1 EMBL· GenBank· DDBJ | mRNA | ||
U87939 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87926 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87927 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87928 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87929 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87930 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87931 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87932 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87933 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87934 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87935 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87936 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87937 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U87938 EMBL· GenBank· DDBJ | AAC39921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CR456365 EMBL· GenBank· DDBJ | CAG30251.1 EMBL· GenBank· DDBJ | mRNA | ||
CR536568 EMBL· GenBank· DDBJ | CAG38805.1 EMBL· GenBank· DDBJ | mRNA | ||
AL023553 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL008582 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC014092 EMBL· GenBank· DDBJ | AAH14092.1 EMBL· GenBank· DDBJ | mRNA | ||
BC026196 EMBL· GenBank· DDBJ | AAH26196.1 EMBL· GenBank· DDBJ | mRNA |