Detail Information for IndEnz0002006372
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