IED ID | IndEnz0002004468 |
Enzyme Type ID | protease004468 |
Protein Name |
Carboxypeptidase G2 CPDG2 EC 3.4.17.11 Folate hydrolase G2 Glutamate carboxypeptidase Pteroylmonoglutamic acid hydrolase G2 Glucarpidase |
Gene Name | cpg2 |
Organism | Pseudomonas sp. (strain RS-16) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Proteobacteria incertae sedis unclassified pseudomonads Pseudomonas sp. (strain RS-16) |
Enzyme Sequence | MRPSIHRTAIAAVLATAFVAGTALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYHSDKAEYVDISAIPRRLYMAARLIMDLGAGK |
Enzyme Length | 415 |
Uniprot Accession Number | P06621 |
Absorption | |
Active Site | ACT_SITE 114; /evidence=ECO:0000250; ACT_SITE 175; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:9083113 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups.; EC=3.4.17.11; |
DNA Binding | |
EC Number | 3.4.17.11 |
Enzyme Function | FUNCTION: Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (16); Chain (1); Helix (15); Metal binding (6); Signal peptide (1); Turn (3) |
Keywords | 3D-structure;Carboxypeptidase;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Pharmaceutical;Protease;Signal;Zinc |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..22 |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 1CG2; 6XJ5; 7M6U; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 43,932 |
Kinetics | |
Metal Binding | METAL 112; /note=Zinc 2; /evidence=ECO:0000269|PubMed:9083113; METAL 141; /note=Zinc 1; /evidence=ECO:0000269|PubMed:9083113; METAL 141; /note=Zinc 2; /evidence=ECO:0000269|PubMed:9083113; METAL 176; /note=Zinc 1; /evidence=ECO:0000269|PubMed:9083113; METAL 200; /note=Zinc 2; /evidence=ECO:0000269|PubMed:9083113; METAL 385; /note=Zinc 1; /evidence=ECO:0000269|PubMed:9083113 |
Rhea ID | |
Cross Reference Brenda | 3.4.17.11; |