| IED ID | IndEnz0002004487 |
| Enzyme Type ID | protease004487 |
| Protein Name |
Carboxypeptidase Y homolog A EC 3.4.16.5 |
| Gene Name | cpyA Pc22g00890 |
| Organism | Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium chrysogenum species complex Penicillium rubens Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
| Enzyme Sequence | MRVLSATLLAGAASAAAPPFQQVLGAHKEYAENVIQQGADAFKPLQHLQDQFKSLSGEARQLWEEVSNYFPESMESAPLLSLPKKHTRRPDSHWDYHVSGAEVQDIWVSGAEGTKEREVDGRLEAYNLRAKKVDPSALGIDPGVKQYSGYLDDDENDKHLFYWFFESRNDPKNDPVVLWLNGGPGCSSLTGLFMELGPSSIDSKIKPVYNDFSWNNNASVIFLDQPINVGYSYSGGSVSDTVAAGKDVYALLTLFFKQFPEYATQDFHIAGESYAGHYIPVMASEILSHKKRNINLKSVLIGNGLTDGLTQYGYYRPMACGEGGYPAVLDESTCQSMDNSLSRCQSMIQACYNSESPWVCVPASIYCNNAMLGPYQRTGQNVYDIRGKCEDESNLCYKGMGYVSEYLGQESVREAVGAEVDGYDSCNFDINRNFLFNGDWFKPYHRLVPGLLEQIPVLIYAGDADFICNWLGNKAWSEALEWPGQKEFASAELEDLKIVQNEHVGKKIGQIKSHGNFTFMRIYGGGHMVPMDQPESGLEFFNRWIGGEWF |
| Enzyme Length | 550 |
| Uniprot Accession Number | B6HPP6 |
| Absorption | |
| Active Site | ACT_SITE 273; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074; ACT_SITE 465; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074; ACT_SITE 527; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074}; |
| DNA Binding | |
| EC Number | 3.4.16.5 |
| Enzyme Function | FUNCTION: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (5); Glycosylation (2); Propeptide (1); Signal peptide (1) |
| Keywords | Carboxypeptidase;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 61,428 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |