P40011 · RRAAH_YEAST
- Protein4-hydroxy-4-methyl-2-oxoglutarate aldolase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids234 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
Miscellaneous
Present with 846 molecules/cell in log phase SD medium.
Catalytic activity
- 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate
Cofactor
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Divalent metal cation. Has preference for nickel ions for the HMG aldolase activity. Has preference for cobalt and zinc ions for the OAA decarboxylase activity.
Activity regulation
Competitively inhibited by oxalate, a pyruvate enolate analog.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
126.5 μM | 4-hydroxy-4-methyl-2-oxoglutarate | |||||
132.5 μM | oxaloacetate |
kcat is 0.0276 sec-1 with 4-hydroxy-4-methyl-2-oxoglutarate as substrate and 3.91 sec-1 with oxaloacetate as substrate.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity | |
Molecular Function | metal ion binding | |
Molecular Function | oxaloacetate decarboxylase activity | |
Biological Process | 3,4-dihydroxybenzoate catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-hydroxy-4-methyl-2-oxoglutarate aldolase
- EC number
- Short namesHMG aldolase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP40011
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000202621 | 2-234 | 4-hydroxy-4-methyl-2-oxoglutarate aldolase | |||
Sequence: SDLQKLQRFSTCDISDGLLNVYNIPTGGYFPNLTAISPPQNSSIVGTAYTVLFAPIDDPRPAVNYIDSVPPNSILVLALEPHLQSQFHPFIKITQAMYGGLMSTRAQYLKSNGTVVFGRIRDVDEHRTLNHPVFAYGVGSCAPKAVVKAVGTNVQLKILTSDGVTQTICPGDYIAGDNNGIVRIPVQETDISKLVTYIEKSIEVDLLVSEDIKNGIPAKQAQNDRRSVLKKYI |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length234
- Mass (Da)25,563
- Last updated1995-02-01 v1
- ChecksumEC109F224240F980
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U18778 EMBL· GenBank· DDBJ | AAB64543.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006939 EMBL· GenBank· DDBJ | DAA07661.1 EMBL· GenBank· DDBJ | Genomic DNA |