D7GCL9 · D7GCL9_PROFC
- Protein2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- GenemenD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids551 (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
- 2-oxoglutarate + H+ + isochorismate = 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 | lyase 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Propionibacteriaceae > Propionibacterium
Accessions
- Primary accessionD7GCL9
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-26 | Disordered | ||||
Sequence: MSNTADPQNPPQARSGEPAAAVGQAV | ||||||
Domain | 37-157 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: LARALVTALVAHGLRDVVYCPGSRDAPFAYALDAAQHAGWLRVAVRLDERAAGFQALGLAKAAAAQGTARPVAVVTTSGTAVANLHPAVLEADAAGVALVVVSADRPHEMWRTGANQTTEQ | ||||||
Region | 216-241 | Disordered | ||||
Sequence: DDQWLPGPAPAPEPHREAPGAPTELP | ||||||
Compositional bias | 218-236 | Pro residues | ||||
Sequence: QWLPGPAPAPEPHREAPGA |
Sequence similarities
Belongs to the TPP enzyme family. MenD subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length551
- Mass (Da)56,476
- Last updated2010-08-10 v1
- Checksum31772F627611F442
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 218-236 | Pro residues | ||||
Sequence: QWLPGPAPAPEPHREAPGA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FN806773 EMBL· GenBank· DDBJ | CBL56280.1 EMBL· GenBank· DDBJ | Genomic DNA |