IED ID | IndEnz0002005876 |
Enzyme Type ID | protease005876 |
Protein Name |
Carboxypeptidase D EC 3.4.17.22 CPD-2 Metallocarboxypeptidase D Fragment |
Gene Name | CPD |
Organism | Lophonetta specularioides (Crested duck) (Anas specularioides) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Anseriformes (ducks geese and swans) Anatidae (waterfowl) Anatinae Lophonetta Lophonetta specularioides (Crested duck) (Anas specularioides) |
Enzyme Sequence | QAVQPVDFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGIHEAGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVQSTRIHIMPSMNPDGYEKSQEGDRGGTVGRNNSNNYDLNRNFPDQFFQVTDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGIAIYSKSPDDAVFQQLALSYSKENKKMYQGSPCKDLYPTEYFPHGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRSLLQFIKQVHRGIWGFVLDATDGRGILNATISVADINHPVTTYKDGDYWRLLVQGTYKVTASARGYDPVTKTVEVDSKGGVQVNFTLSRT |
Enzyme Length | 380 |
Uniprot Accession Number | P83852 |
Absorption | |
Active Site | ACT_SITE 269; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14384 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Releases C-terminal Arg and Lys from polypeptides.; EC=3.4.17.22; Evidence={ECO:0000250|UniProtKB:Q90240}; |
DNA Binding | |
EC Number | 3.4.17.22 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (18); Chain (1); Disulfide bond (1); Glycosylation (3); Helix (14); Metal binding (3); Non-terminal residue (2); Region (2); Turn (5) |
Keywords | 3D-structure;Carboxypeptidase;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 1H8L; 1QMU; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 43,292 |
Kinetics | |
Metal Binding | METAL 71; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:10545093; METAL 74; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:10545093; METAL 178; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:10545093 |
Rhea ID | |
Cross Reference Brenda |