P17109 · MEND_ECOLI
- Protein2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- GenemenD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids556 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
53 nM | isochorismate | 7.8 | 22.5 | |||
1.5 μM | 2-oxoglutarate | 7.8 | 22.5 | |||
2.4 μM | thiamine diphosphate | 7.8 | 22.5 | |||
80 μM | magnesium ions | 7.8 | 22.5 |
pH Dependence
Optimum pH is 7-8.
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 | protein homodimerization activity | |
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP17109
- Secondary accessions
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 55 | Loss of activity. | ||||
Sequence: E → Q |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000090829 | 1-556 | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase | |||
Sequence: MSVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTLHAGGVHINCPFAEPLYGEMDDTGLSWQQRLGDWWQDDKPWLREAPRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDVLSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKRQPWCVEIPRLAEQAMQAVIARRDAFGEAQLAHRICDYLPEQGQLFVGNSLVVRLIDALSQLPAGYPVYSNRGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNGGQIFSLLPTPQSERERFYLMPQNVHFEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIEMVVNDTDGAQTLQQLLAQVSHL |
Proteomic databases
Expression
Induction
By isopropyl-beta-D-thiogalactoside (IPTG).
Structure
Sequence
- Sequence statusComplete
- Length556
- Mass (Da)61,367
- Last updated1997-11-01 v4
- Checksum278201D02243E76D
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 42 | in Ref. 5; AAA24153 | ||||
Sequence: Missing | ||||||
Sequence conflict | 163-183 | in Ref. 5; AAA24153 | ||||
Sequence: GVHINCPFAEPLYGEMDDTGL → ESISTARLLNRCMAKWTIPGF | ||||||
Sequence conflict | 398 | in Ref. 5; AAA24153 | ||||
Sequence: Missing | ||||||
Sequence conflict | 543-556 | in Ref. 6; AAB59060 | ||||
Sequence: AQTLQQLLAQVSHL → RKRSSNFWRR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U54790 EMBL· GenBank· DDBJ | AAC44304.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC75324.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA16089.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21787 EMBL· GenBank· DDBJ | AAA24153.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
L04464 EMBL· GenBank· DDBJ | AAB59060.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L35030 EMBL· GenBank· DDBJ | AAA24150.1 EMBL· GenBank· DDBJ | Genomic DNA |