IED ID | IndEnz0002016201 |
Enzyme Type ID | protease016201 |
Protein Name |
Hydrogenase 3 maturation protease EC 3.4.23.51 HycI protease |
Gene Name | hycI Z4025 ECs3573 |
Organism | Escherichia coli O157:H7 |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O157:H7 |
Enzyme Sequence | MTDVLLCVGNSMMGDDGAGPLLAEKCAAAPKGNWVVIDGGSAPENDIVAIRELRPTRLLIVDATDMGLNPGEIRIIDPDDIAEMFMMTTHNMPLNYLIDQLKEDIGEVIFLGIQPDIVGFYYPMTQPIKDAVETVYQRLEGWEGNGGFAQLAVEEE |
Enzyme Length | 156 |
Uniprot Accession Number | P0AEW0 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=This enzyme specifically removes a 32-amino acid peptide from the C-terminus of the precursor of the large subunit of E.coli hydrogenase 3 by cleavage at the C-terminal side of Arg-537.; EC=3.4.23.51; Evidence={ECO:0000250|UniProtKB:P0AEV9}; |
DNA Binding | |
EC Number | 3.4.23.51 |
Enzyme Function | FUNCTION: Protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3. {ECO:0000250|UniProtKB:P0AEV9}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Initiator methionine (1); Metal binding (3) |
Keywords | Aspartyl protease;Hydrolase;Metal-binding;Nickel;Protease;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 17,057 |
Kinetics | |
Metal Binding | METAL 16; /note=Nickel; /evidence=ECO:0000250; METAL 62; /note=Nickel; /evidence=ECO:0000250; METAL 90; /note=Nickel; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |