| IED ID | IndEnz0002011635 |
| Enzyme Type ID | protease011635 |
| Protein Name |
Glutamate 5-kinase 1 EC 2.7.2.11 Gamma-glutamyl kinase 1 GK 1 |
| Gene Name | proB BSU13120 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MKKQRIVVKIGSSSLTNSKGSIDEAKIREHVQAISVLKKAGHEMILITSGAVAAGFSSLGYPSRPVTIKGKQAAAAVGQTLLMQQYMNQFKQYSLTPGQILLTRNDFSKRERYRNAYATIMELLERGVIPIINENDSTSVEELTFGDNDMLSALVSGLIHADQLMILTDINGLYDANPNENPEAKRFDYLPEITPELLGYAGSAGSKVGTGGMKSKLLATQTALSLGVKVFIGTGSGEQKLADILDGRGDGTYIGDKELSSVNNTRQWIQFHSPISGEIIIDAGAEEAMIHNGSSLLPAGVVGVNGSFPKGAVVEVRGPGGVIGKGQTHYSSEEIMEAKGKRSDELDFEKTFEVIHRNDWVNVKD |
| Enzyme Length | 365 |
| Uniprot Accession Number | P39820 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 9; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00456; BINDING 49; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00456; BINDING 136; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00456; BINDING 148; /note=Substrate; via amide nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_00456 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00456}; |
| DNA Binding | |
| EC Number | 2.7.2.11 |
| Enzyme Function | FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00456}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00456}. |
| nucleotide Binding | NP_BIND 168..169; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00456; NP_BIND 210..216; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00456 |
| Features | Binding site (4); Chain (1); Domain (1); Nucleotide binding (2); Sequence conflict (5) |
| Keywords | ATP-binding;Amino-acid biosynthesis;Cytoplasm;Direct protein sequencing;Kinase;Nucleotide-binding;Proline biosynthesis;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00456}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,346 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:14877 |
| Cross Reference Brenda |