Detail Information for IndEnz0002002605
IED ID IndEnz0002002605
Enzyme Type ID protease002605
Protein Name Hydrogenase 3 maturation protease
EC 3.4.23.51
HycI protease
Gene Name hycI b2717 JW2687
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MTDVLLCVGNSMMGDDGAGPLLAEKCAAAPKGNWVVIDGGSAPENDIVAIRELRPTRLLIVDATDMGLNPGEIRIIDPDDIAEMFMMTTHNMPLNYLIDQLKEDIGEVIFLGIQPDIVGFYYPMTQPIKDAVETVYQRLEGWEGNGGFAQLAVEEE
Enzyme Length 156
Uniprot Accession Number P0AEV9
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:0000269|PubMed:10727938};
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:0000269|PubMed:10727938}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (6); Chain (1); Helix (8); Initiator methionine (1); Metal binding (3); Mutagenesis (3); Turn (2)
Keywords 3D-structure;Aspartyl protease;Direct protein sequencing;Hydrolase;Metal-binding;Nickel;Protease;Reference proteome
Interact With P0AFG8
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D NMR spectroscopy (1); X-ray crystallography (1)
Cross Reference PDB 2E85; 2I8L;
Mapped Pubmed ID 15690043; 16606699;
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 3.4.23.51;