B0YD89 · PRPC_ASPFC
- Protein2-methylcitrate synthase, mitochondrial
- GenemcsA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids465 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the methylcitrate cycle that catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate. Plays an important role in detoxification of propionyl-CoA, an inhibitor of both primary and secondary metabolism. Has also citrate synthase activity using as substrates acetyl-CoA and oxaloacetate. Plays a key role in the estabishment of invasive pulmonary aspergillosis.
Catalytic activity
- H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate + CoA + H+
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
4.7 μM | propionyl-CoA | |||||
5 μM | acetyl-CoA | |||||
4.9 μM | oxaloacetate |
Pathway
Organic acid metabolism; propanoate degradation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 74 | CoA (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain B | ||||
Sequence: R | ||||||
Binding site | 192 | CoA (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain A | ||||
Sequence: K | ||||||
Binding site | 269 | oxaloacetate (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain A | ||||
Sequence: H | ||||||
Binding site | 304 | CoA (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain B | ||||
Sequence: L | ||||||
Active site | 305 | |||||
Sequence: H | ||||||
Binding site | 346 | CoA (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain B | ||||
Sequence: V | ||||||
Binding site | 348 | CoA (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain B | ||||
Sequence: G | ||||||
Binding site | 349 | CoA (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain B | ||||
Sequence: Y | ||||||
Active site | 351 | |||||
Sequence: H | ||||||
Binding site | 351 | oxaloacetate (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain A | ||||
Sequence: H | ||||||
Binding site | 360 | oxaloacetate (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain A | ||||
Sequence: R | ||||||
Binding site | 400 | CoA (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain B | ||||
Sequence: T | ||||||
Binding site | 401 | CoA (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain B | ||||
Sequence: K | ||||||
Binding site | 406 | CoA (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain B | ||||
Sequence: N | ||||||
Active site | 408 | |||||
Sequence: D | ||||||
Binding site | 434 | oxaloacetate (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain A | ||||
Sequence: R | ||||||
Binding site | 454 | oxaloacetate (UniProtKB | ChEBI); ligand shared between homodimeric partners; in chain B | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | 2-methylcitrate synthase activity | |
Molecular Function | citrate (Si)-synthase activity | |
Biological Process | propionate catabolic process, 2-methylcitrate cycle | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-methylcitrate synthase, mitochondrial
- EC number
- Short namesMethylcitrate synthase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionB0YD89
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Leads to attenuated virulence in a mouse model for pulmonary infection and an infection model based on embryonated eggs.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 81 | No activity. | ||||
Sequence: W → Y | ||||||
Mutagenesis | 352 | Increased affinity for oxaloacetate, acetyl-coA and propionyl-CoA. | ||||
Sequence: G → A | ||||||
Mutagenesis | 419 | No activity. | ||||
Sequence: G → A |
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-29 | Mitochondrion | ||||
Sequence: MAMTMRSTRHASKLAQTARLALTNSRRYS | ||||||
Chain | PRO_0000432972 | 30-465 | 2-methylcitrate synthase, mitochondrial | |||
Sequence: TAEPDLKTALKAVIPAKRELFKQVKERSDEVIGEVKVANVIGGMRGLKSMLWEGSVLDPEEGIRFHGKTIKDCQKELPKGTSGTEMLPEAMFWLLLTGQVPSTNQVRAFSRELAEQSHLPQHILDLIKSFPRSMHPMTQLSIAVAALNTESKFAKAYEKGLSKADYWEPTFDDSISLLAKIPRVAALVFRPDEVDQVGTQALDASQDWSYNFAELLGKGGKENQDFHDLLRLYLALHGDHEGGNVSAHATHLVGSALSDPFLSYSAGLLGLAGPLHGLAAQEVLRWILAMQDKIGTKFTDDDVRNYLWDTLKSGRVVPGYGHGVLRKPDPRFQALMDFAATRPDVLANPVFQLVKKNSEIAPAVLTEHGKTKNPHPNVDAASGVLFYHYGFQQPLYYTVTFGVSRALGPLVQLIWDRALGLPIERPKSINLLGLKK |
Expression
Induction
Expression is induced by peptone and during infection.
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length465
- Mass (Da)51,412
- Last updated2008-04-08 v1
- ChecksumB4A4C5903B04E125
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS499602 EMBL· GenBank· DDBJ | EDP47623.1 EMBL· GenBank· DDBJ | Genomic DNA |