IED ID | IndEnz0002003257 |
Enzyme Type ID | protease003257 |
Protein Name |
Alkaline phosphatase isozyme conversion protein EC 3.4.11.- |
Gene Name | iap b2753 JW2723 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MFSALRHRTAALALGVCFILPVHASSPKPGDFANTQARHIATFFPGRMTGTPAEMLSADYIRQQFQQMGYRSDIRTFNSRYIYTARDNRKSWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPLSDADADANLGGLTLQGMDDNAAGLGVMLELAERLKNTPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGDKLYFNSGVKTPEAVRKLTRDRALAIARSHGIAATTNPGLNKNYPKGTGCCNDAEIFDKAGIAVLSVEATNWNLGNKDGYQQRAKTPAFPAGNSWHDVRLDNHQHIDKALPGRIERRCRDVMRIMLPLVKELAKAS |
Enzyme Length | 345 |
Uniprot Accession Number | P10423 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.11.- |
Enzyme Function | FUNCTION: This protein, presumably an aminopeptidase, mediates the conversion of E.coli alkaline phosphatase isozyme 1, to isozymes 2 and 3 by removing, one by one, the two N-terminal arginine residues. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Metal binding (5); Signal peptide (1) |
Keywords | Aminopeptidase;Hydrolase;Metal-binding;Protease;Reference proteome;Signal;Zinc |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000305 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 6295883; 7002151; |
Motif | |
Gene Encoded By | |
Mass | 37,920 |
Kinetics | |
Metal Binding | METAL 117; /note=Zinc 1; /evidence=ECO:0000250; METAL 143; /note=Zinc 1; /evidence=ECO:0000250; METAL 143; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 176; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 204; /note=Zinc 1; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |