Detail Information for IndEnz0002000080
IED ID IndEnz0002000080
Enzyme Type ID protease000080
Protein Name Phosphoglycerate kinase
EC 2.7.2.3
Gene Name pgk SPD_0445
Organism Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pneumoniae Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Enzyme Sequence MAKLTVKDVDLKGKKVLVRVDFNVPLKDGVITNDNRITAALPTIKYIIEQGGRAILFSHLGRVKEESDKAGKSLAPVAADLAAKLGQDVVFPGVTRGAELEAAINALEDGQVLLVENTRYEDVDGKKESKNDPELGKYWASLGDGIFVNDAFGTAHRAHASNVGISANVEKAVAGFLLENEIAYIQEAVETPERPFVAILGGSKVSDKIGVIENLLEKADKVLIGGGMTYTFYKAQGIEIGNSLVEEDKLDVAKALLEKANGKLILPVDSKEANAFAGYTEVRDTEGEAVSEGFLGLDIGPKSIAKFDEALTGAKTVVWNGPMGVFENPDFQAGTIGVMDAIVKQPGVKSIIGGGDSAAAAINLGRADKFSWISTGGGASMELLEGKVLPGLAALTEK
Enzyme Length 398
Uniprot Accession Number Q04LZ5
Absorption
Active Site
Activity Regulation
Binding Site BINDING 36; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00145; BINDING 119; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00145; BINDING 157; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00145; BINDING 208; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00145; BINDING 296; /note=ATP; via carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_00145; BINDING 327; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00145
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00145};
DNA Binding
EC Number 2.7.2.3
Enzyme Function
Temperature Dependency
PH Dependency
Pathway PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_00145}.
nucleotide Binding NP_BIND 354..357; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00145
Features Beta strand (16); Binding site (6); Chain (1); Helix (22); Nucleotide binding (1); Region (2); Turn (4)
Keywords 3D-structure;ATP-binding;Cytoplasm;Glycolysis;Kinase;Nucleotide-binding;Transferase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3ZLB;
Mapped Pubmed ID 24196407;
Motif
Gene Encoded By
Mass 41,939
Kinetics
Metal Binding
Rhea ID RHEA:14801
Cross Reference Brenda