A0A068MT64 · A0A068MT64_SYNY4
- Protein2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- GenemenD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids596 (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
Cofactor biosynthesis; phylloquinone biosynthesis.
Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
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 | |
Biological Process | phylloquinone biosynthetic process |
Keywords
- Molecular function
- 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
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Merismopediaceae > Synechocystis
Accessions
- Primary accessionA0A068MT64
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-125 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: ASLLVETLFRLGLRQAVICPGSRSSPLTVALARHGEIDCVVSLDERSASFFALGYGKRTGKPALLVCTSGTAAANFLPAIIEAHYSQVPLLVLTGDRPPKLRHCRAGQTIDQTK | ||||||
Domain | 424-554 | Thiamine pyrophosphate enzyme TPP-binding | ||||
Sequence: WLEFFWPANGDRHRIFVNRGANGIDGTLSTAMGISHRSIHQTVLLTGDLSLLHDSNGFLNQSQMRGNLTIILLNNNGGGIFQTLPIAQCEDVFETYFATPQSVDFAQLCGTYGVDHHVITDLGSLKEQLET |
Sequence similarities
Belongs to the TPP enzyme family. MenD subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length596
- Mass (Da)66,097
- Last updated2014-10-01 v1
- Checksum2AE0837D6143F6D4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP007542 EMBL· GenBank· DDBJ | AIE73149.1 EMBL· GenBank· DDBJ | Genomic DNA |