IED ID | IndEnz0002006372 |
Enzyme Type ID | protease006372 |
Protein Name |
Enolase EC 4.2.1.11 2-phospho-D-glycerate hydro-lyase 2-phosphoglycerate dehydratase |
Gene Name | eno NMB1285 |
Organism | Neisseria meningitidis serogroup B (strain MC58) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Neisseriales Neisseriaceae Neisseria Neisseria meningitidis Neisseria meningitidis serogroup B Neisseria meningitidis serogroup B (strain MC58) |
Enzyme Sequence | MSAIVDIFAREILDSRGNPTVECDVLLESGVMGRAAVPSGASTGQKEALELRDGDKSRYSGKGVLKAVEHVNNQIAQALIGIDANEQSYIDQIMIELDGTENKGNLGANATLAVSMAVARAAAEDSGLPLYRYLGGAGPMSLPVPMMNVINGGEHANNSLNIQEFMIMPVGAKSFREALRCGAEIFHALKKLCDSKGFPTTVGDEGGFAPNLNSHKEALQLMVEATEAAGYKAGEDVLFALDCASSEFYKDGKYHLEAEGRSYTNAEFAEYLEGLVNEFPIISIEDGMDENDWEGWKLLTEKLGGRVQLVGDDLFVTNPKILAEGIEKGVANALLVKVNQIGTLSETLKAVDLAKRNRYASVMSHRSGETEDSTIADLAVATNCMQIKTGSLSRSDRMAKYNQLLRIEEELAEAADYPSKAAFYQLGK |
Enzyme Length | 428 |
Uniprot Accession Number | Q9JZ53 |
Absorption | |
Active Site | ACT_SITE 205; /note=Proton donor; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; ACT_SITE 337; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_00318 |
Activity Regulation | ACTIVITY REGULATION: The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}. |
Binding Site | BINDING 155; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 164; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 285; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 312; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 337; /note=Substrate; covalent; in inhibited form; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 388; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; |
DNA Binding | |
EC Number | 4.2.1.11 |
Enzyme Function | FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}. |
nucleotide Binding | |
Features | Active site (2); Binding site (6); Chain (1); Metal binding (3); Region (1) |
Keywords | Cytoplasm;Glycolysis;Lyase;Magnesium;Metal-binding;Reference proteome;Secreted |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 46,134 |
Kinetics | |
Metal Binding | METAL 242; /note=Magnesium; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; METAL 285; /note=Magnesium; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; METAL 312; /note=Magnesium; /evidence=ECO:0000255|HAMAP-Rule:MF_00318 |
Rhea ID | RHEA:10164 |
Cross Reference Brenda |