Protein Information

General Information
MoonProt ID332
First appeared in release2.0
Name(s)enolase, 2-phospho-D-glycerate hydro-lyase, 2-phosphoglycerate dehydratase Gene: eno
UniProt IDI7WI49 (I7WI49_STRCB)
GO termsGO:0006096 glycolytic process GO:0000287 magnesium ion binding GO:0004634 phosphopyruvate hydratase activity GO:0016829 lyase activity GO:0046872 metal ion binding GO:0000015 phosphopyruvate hydratase complex GO:0005576 extracellular region GO:0005737 cytoplasm GO:0009986 cell surface GO:0005515 protein binding
Organisms for which functions have been demonstratedStreptococcus canis, group G Streptococci
Sequence length435 amino acids
FASTA sequence>tr|I7WI49|I7WI49_STRCB Enolase OS=Streptococcus canis FSL Z3-227 GN=eno PE=3 SV=1 MSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGASTGEHEAVELRDGDKSRYLGLGTQKAVDNVNNIIAEAIIGYDVRDQQAIDRAMIALDGTPNKGKLGANAILGVSIAVARAAADYLEVPLYTYLGGFNTKVLPTPMMNIINGGSHSDAPIAFQEFMIMPVGAPTFKEGLRWGAEVFHALKKILKERGLVTAVGDEGGFAPKFEGTEDGVETILKAIEAAGYEAGENGIMIGFDCASSEFYDKERKVYDYTKFEGEGAAVRTSAEQIDYLEELVNKYPIITIEDGMDENDWDGWKALTERLGGRVQLVGDDFFVTNTEYLARGIKENAANSILIKVNQIGTLTETFEAIEMAKEAGYTAVVSHRSGETEDSTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDQLGEVAQYKGIKSFYNLKK
Structure Information
PDB IDseveral from Group A streptococcus
Quaternary structure
Function 1
Function descriptionenolase, in glycolysis, 2-phospho-D-glycerate hydro-lyase, 2-phosphoglycerate dehydratase
References for functionLef├ębure, Tristan, et al. "Gene repertoire evolution of Streptococcus pyogenes inferred from phylogenomic analysis with Streptococcus canis and Streptococcus dysgalactiae." PloS one7.5 (2012): e37607.
E.C. number4.2.1.11
Location of functional site(s)binding site: 155, 164, 292, 319, 344, 395; active site: 205, 344; metal binding: 243, 292, 319
Cellular location of functioncytoplasm
Comments
Function 2
Function descriptionplasminogen binding
References for function23481605
E.C. number
Location of functional site(s)
Cellular location of function
Commentsbinds to first 4 kringle domains of plasminogen, secretion of enolase and reassociation to surface