General Information |
MoonProt ID | 45 |
First appeared in release | 1.0 |
Name(s) | enolase
?-enolase
2-phospho-D-glycerate hydrolase
2-phosphoglycerate dehydratase
Gene Name: eno |
UniProt ID | D8H2L1 (D8H2L1_BACAI), Unreviewed |
GO terms | GO:0006096 glycolysis
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 |
Organisms for which functions have been demonstrated | Bacillus anthracis |
Sequence length | 431 |
FASTA sequence | >gi|59797626|sp|Q81X78.1|ENO_BACAN RecName: Full=Enolase; AltName: Full=2-phospho-D-glycerate hydro-lyase; AltName: Full=2-phosphoglycerate dehydratase
MSTIIDVYAREVLDSRGNPTVEVEVYTESGAFGRAIVPSGASTGEHEAVELRDGDKSRYLGKGVMNAVNNVNEAIAPEIVGFDVTDQAGIDRAMIELDGTPNKGKLGANAILGVSMAVAHAAADFVGLPLYRYLGGFNAKQLPTPMMNIINGGSHADNNVDFQEFMILPVGAPTFKESIRMGAEVFHALKAVLHDKGLNTAVGDEGGFAPNLGSNREALEVIIEAIEKAGYKAGENVFLGMDVASSEFYNKETGKYDLAGEGRTGLTSAEMVDFYEELCKDFPIISIEDGLDENDWDGHKLLTERIGDKVQLVGDDLFVTNTQKLAEGIEKGISNSILIKVNQIGTLTETFEAIEMAKRAGYTAVVSHRSGETEDATIADIAVATNAGQIKTGSMSRTDRIAKYNQLLRIEDELGEIAVYDGIKSFYNIKR
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Structure Information |
PDB ID | closest is Bacillus with 74% amino acid sequence identity |
Quaternary structure | |
SCOP | NA |
CATH | NA |
TM Helix Prediction | no TM helices |
DisProt Annotation | Not in DisProt |
Predicted Disorder Regions | 1-4, 41-43,428-431 |
Connections to Disease |
OMIM ID | |
Function 1 |
Function description | enolase, enzyme
2-phospho-D-glycerate => phosphoenolpyruvate + H2O
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate
Carbohydrate degradation, glycolysis |
References for function | |
E.C. number | 4.2.1.11 |
Location of functional site(s) | |
Cellular location of function | cytoplasm |
Comments | |
Function 2 |
Function description | binds plasminogen and laminin |
References for function | Agarwal S, Kulshreshtha P, Bambah Mukku D, Bhatnagar R: Alpha-enolase
binds to human plasminogen on the surface of Bacillus anthracis.
Biochim Biophys Acta. 2008 Jul-Aug;1784(7-8):986-94. doi: 10.1016/j.bbapap.2008.03.017. Epub 2008 Apr 16. PMID: 18456007
|
E.C. number | N/A |
Location of functional site(s) | |
Cellular location of function | cell surface |
Comments | |