| IED ID | IndEnz0002006034 |
| Enzyme Type ID | protease006034 |
| Protein Name |
Glutamate decarboxylase beta GAD-beta EC 4.1.1.15 |
| Gene Name | gadB b1493 JW1488 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MDKKQVTDLRSELLDSRFGAKSISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKLGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT |
| Enzyme Length | 466 |
| Uniprot Accession Number | P69910 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 62; /note=Substrate; BINDING 83; /note=Substrate; BINDING 212; /note=Pyridoxal phosphate; BINDING 275; /note=Pyridoxal phosphate |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2; Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15; |
| DNA Binding | |
| EC Number | 4.1.1.15 |
| Enzyme Function | FUNCTION: Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (17); Binding site (4); Chain (1); Helix (20); Modified residue (4); Mutagenesis (2); Region (1); Turn (6) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;Decarboxylase;Direct protein sequencing;Lyase;Membrane;Pyridoxal phosphate;Reference proteome |
| Interact With | P36879 |
| Induction | INDUCTION: By acidic conditions. Expression is regulated by a complex system involving RpoS, cAMP, CRP, EvgAS, H-NS, GadE, GadW and GadX. The level of involvement for each regulator varies depending upon the growth phase and the medium. {ECO:0000269|PubMed:10383761, ECO:0000269|PubMed:11976288, ECO:0000269|PubMed:12399493, ECO:0000269|PubMed:12446650, ECO:0000269|PubMed:12694615, ECO:0000269|PubMed:12867478, ECO:0000269|PubMed:12940989}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12912902}. Membrane {ECO:0000269|PubMed:12912902}. Note=Localized exclusively in the cytoplasm at neutral pH, but is recruited to the membrane when the pH falls. |
| Modified Residue | MOD_RES 276; /note=N6-(pyridoxal phosphate)lysine; MOD_RES 446; /note=N6-acetyllysine; /evidence=ECO:0000269|PubMed:18723842; MOD_RES 453; /note=N6-acetyllysine; /evidence=ECO:0000269|PubMed:18723842; MOD_RES 464; /note=N6-acetyllysine; /evidence=ECO:0000269|PubMed:18723842 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 1PMM; 1PMO; 2DGK; 2DGL; 2DGM; 3FZ6; 3FZ7; 3FZ8; |
| Mapped Pubmed ID | 15690043; 16606699; 16675957; 16858726; 19440203; 24561554; 7608084; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,668 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17785 |
| Cross Reference Brenda | 4.1.1.15; |