A0A150AU89 · A0A150AU89_BACCE
- Protein2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- GenemenD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids584 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic activity
- isochorismate + 2-oxoglutarate + H+ = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 1 thiamine pyrophosphate per subunit.
Pathway
Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Quinol/quinone metabolism; menaquinone biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | manganese ion binding | |
Molecular Function | thiamine pyrophosphate binding | |
Biological Process | menaquinone biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- EC number
- Short namesSEPHCHC synthase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillati > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Accessions
- Primary accessionA0A150AU89
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 14-125 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | |||
Domain | 222-403 | Menaquinone biosynthesis protein MenD middle | |||
Domain | 438-553 | Thiamine pyrophosphate enzyme TPP-binding | |||
Sequence similarities
Belongs to the TPP enzyme family. MenD subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length584
- Mass (Da)64,984
- Last updated2016-07-06 v1
- MD5 ChecksumE56CB4A0D400F3FC7AFFD54954EE8391
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LOMT01000161 EMBL· GenBank· DDBJ | KXX85041.1 EMBL· GenBank· DDBJ | Genomic DNA |