Protein Information

General Information
MoonProt ID44
First appeared in release1.0
Name(s)enolase 2-phospho-D-glycerate hydrolase
UniProt IDA5JQI1 (A5JQI1_PARBR), Unreviewed
GO termsGO:0006096 glycolysis GO:0000287 magnesium ion binding GO:0004634 phosphopyruvate hydratase activity GO:0016829 lyase activity GO:0000015 phosphopyruvate hydratase complex GO:0098631 cell adhesion mediator GO:0005515 protein binding
Organisms for which functions have been demonstratedParacoccidioides brasiliensis
Sequence length438
FASTA sequence>gi|146762537|gb|ABQ45367.1| enolase [Paracoccidioides brasiliensis] MAITKIHARSVYDSRGNPTVEVDVVTETGLHRAIVPSGASTGQHEACELRDGDQSKWLGKGVLNAVKNVNSVIGPAIIKENIDVKDQSKVDEFLNKLDGTPNKSKLGANAILGVSLAIAKAGAAEKGVPLYAHVSDLAGTKKPYVLPVPFQNVLNGGSHAGGRLAFQEFMIVPTAAPSFSEALRQGSEVYHKLKALAKKKYGQSAGNVGDEGGVAPDIQTPEEALDLITEAIEQAGYTGQVKIALDIASSEFYKADEKKYDLDFKNPDSDKSKWLTYEQLADLYKKLASKYAIVSIEDPFAEDDWEAWSYYFKTCDLQVVADDLTVTNPIRIKKAIELKSCNALLLKVNQIGTLTESIQAAKDSYAAGWGVMVSHRSGETEDVTIADIVVGLRAGQIKTGAPARSERLAKLNQILRIEEELGSNAVYAGDKFRAAINM
Structure Information
PDB ID
Quaternary structure
Function 1
Function descriptionenolase, enzyme catalyses the dehydration of 2-phospho-D-glycerate (PGA) to phosphoenolpyruvate glycolysis, gluconeogenesis
References for function
E.C. number4.2.1.11
Location of functional site(s)Active site:211,347 Binding site:159,297,398,322,168
Cellular location of functioncytoplasm
Comments
Function 2
Function descriptionfibronectin binding
References for functionDonofrio FC, Calil AC, Miranda ET, Almeida AM, Benard G, Soares CP, Veloso SN, Soares CM, Mendes Giannini. Enolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding protein.J Med Microbiol. 2009 Jun;58(Pt 6):706-13. doi: 10.1099/jmm.0.003830-0. PMID: 19429745
E.C. numberN/A
Location of functional site(s)
Cellular location of functioncell surface
Comments