_EC 2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid 7 PDB entries  
EC 2.-.-.- Transferases. [17,952 PDB entries]
EC 2.2.-.- Transferring aldehyde or ketone residues. [107 PDB entries]
EC 2.2.1.- Transketolases and transaldolases. [107 PDB entries]
EC 2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid [7 PDB entries]    
2jla

Reaction: Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl- cyclohex-3-ene-1-carboxylate + CO(2).
 


Isochorismate
+
2-oxoglutarate
=
5-enolpyruvoyl-6-hydroxy-2-succinyl- cyclohex-3-ene-1-carboxylate
+
CO(2)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Sephchc synthase.
Cofactor(s): Mg(2+).
Comments: Involved in the biosynthesis of vitamin K(2) (menaquinone). In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO(2) but it is now known that two separate enzymes are involved: this enzyme and Ec 4.2.99.20. Under basic conditions, the product can spontaneously lose pyruvate to form Shchc.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 7 PDB entries in enzyme class E.C.2.2.1.9

  PDB code Protein
2jla
Crystal structure of e.Coli mend, 2-succinyl-5-enolpyruvyl- 6-hydroxy-3-cyclohexadiene-1-carboxylate synthase - semet protein
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (556 residues) CATH domains: 3.40.50.970 Unassigned 3.40.50.970
2jlc
Crystal structure of e.Coli mend, 2-succinyl-5-enolpyruvyl- 6-hydroxy-3-cyclohexadiene-1-carboxylate synthase - native protein
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (554 residues) CATH domains: 3.40.50.970 Unassigned 3.40.50.970
2x7j
Structure of the menaquinone biosynthesis protein mend from bacillus subtilis
Source: Bacillus subtilis. Organism_taxid: 1423. Atcc: 23857. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (579 residues) CATH domain: 3.40.50.970
Bound ligand:   Het Group EDO is 40.00% similar to enzyme reactant 2-oxoglutarate
3flm
Crystal structure of mend from e.Coli
Source: Escherichia coli k-12. Organism_taxid: 83333. Gene: b2264, jw5374, mend. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (535 residues) CATH domains: 3.40.50.970 Unassigned 3.40.50.970
3hww
Crystal structure of menaquinone synthesis protein mend from in complex with oxoglutarate
Source: Escherichia coli k-12. Organism_taxid: 83333. Gene: b2264, jw5374, mend. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, D (539 residues) CATH domains: 3.40.50.970 Unassigned 3.40.50.970
Bound ligand:   Het Group AKG corresponds to enzyme reactant 2-oxoglutarate
3hwx
Crystal structure of menaquinone synthesis protein mend from in complex with thdp
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b2264, jw5374, mend. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, I, J, R, S, Z, 1 (555 residues) CATH domains: 3.40.50.970 Unassigned 3.40.50.970
Bound ligand:   Het Group GOL is 45.45% similar to enzyme reactant 2-oxoglutarate
3lq1
Crystal structure of 2-succinyl-6-hydroxy-2,4-cyclohexadiene 1-carboxylic acid synthase/2-oxoglutarate decarboxylase from listeria monocytogenes str. 4b f2365
Source: Listeria monocytogenes. Organism_taxid: 265669. Strain: 4b f2365. Gene: mend, lmof2365_1699, prk07449. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (513 residues) CATH domain: 3.40.50.970