IED ID | IndEnz0002003978 |
Enzyme Type ID | protease003978 |
Protein Name |
Hydrogenase 2 maturation protease EC 3.4.23.- |
Gene Name | hybD b2993 JW2961 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MRILVLGVGNILLTDEAIGVRIVEALEQRYILPDYVEILDGGTAGMELLGDMANRDHLIIADAIVSKKNAPGTMMILRDEEVPALFTNKISPHQLGLADVLSALRFTGEFPKKLTLVGVIPESLEPHIGLTPTVEAMIEPALEQVLAALRESGVEAIPREAIHD |
Enzyme Length | 164 |
Uniprot Accession Number | P37182 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: Protease involved in the C-terminal processing of HybC, the large subunit of hydrogenase 2. Specifically cleaves off a 15 amino acid peptide from the C-terminus of the precursor of HybC. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (6); Chain (1); Helix (8); Metal binding (3); Sequence conflict (1); Turn (1) |
Keywords | 3D-structure;Aspartyl protease;Hydrolase;Metal-binding;Nickel;Protease;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1CFZ; |
Mapped Pubmed ID | 16606699; 24561554; 7851435; 9738917; |
Motif | |
Gene Encoded By | |
Mass | 17,751 |
Kinetics | |
Metal Binding | METAL 16; /note=Nickel; METAL 62; /note=Nickel; METAL 93; /note=Nickel |
Rhea ID | |
Cross Reference Brenda | 3.4.23.B20; |