A0A0T0MJE0 · A0A0T0MJE0_9CELL
- Protein2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- GenemenD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids613 (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 | 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 > Actinomycetota > Actinomycetes > Micrococcales > Cellulomonadaceae > Cellulomonas
Accessions
- Primary accessionA0A0T0MJE0
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-153 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: TAARVLVQTLATLGVEDVVLAPGSRSAPLAYALADAARPDDERPTGAPRLRLHVRVDERSAAFLAVGLTRASAHGTDDQQHAPRPVAVVTTSGTAVANLHPAVLEAHHSGLPLILLTADRPHELRGTGANQTTDQVG | ||||||
Domain | 447-582 | Thiamine pyrophosphate enzyme TPP-binding | ||||
Sequence: WDSPPVVMANRGLAGIDGTVSTAVGVALGMPERRVRALLGDLTFLHDVGGLLRGPLEAQVHLQLVVANDDGGSIFATLEPGEPDRADVFERVFGTPHGADLAALCAGYGVRHTRVSDVDGLLPALAAPGPGLSVVE |
Sequence similarities
Belongs to the TPP enzyme family. MenD subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length613
- Mass (Da)63,055
- Last updated2016-02-17 v1
- ChecksumFD842F3F9C020DD8
Keywords
- Technical term