| IED ID | IndEnz0002005872 |
| Enzyme Type ID | protease005872 |
| Protein Name |
Cytosolic carboxypeptidase-like protein 5 EC 3.4.17.- EC 3.4.17.24 ATP/GTP-binding protein-like 5 Protein deglutamylase CCP5 |
| Gene Name | agbl5 ccp5 |
| Organism | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Silurana Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Enzyme Sequence | MEVRCGGLLFSSKFDSGNLARVEKVEKPGAEGDAFSGSVSGGSVPTPDYEFNIWTKPDCAETEYENGNRSWFYFSVRFGAPGKLIKINIMNMNKQSKLYSQGMAPFVRTVPIRSRWERIRDRPTFEMVENQFILSFVHRFLDCRGSTTYFAFCFPFSYEESQELMAGLDDRFSDCKNITPGSFPDSIYYHRELLCHSLDGLRVDLLTISSCHGMTEEREPRLDKLFPDRSTPRPYRFTGKRVYFLSSRVHPGETPSSFVFNGFLEFILRQDDPRAQMLRRMFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLNPDFELHPSVYAAKTVLLYHHVYNSVGPNDPDWRTSVSLQTSNISLCPKTSNHSLKDLPLEDSLSELEKANNLLNSMEKEECYITCPQAVTQGAPPENDPNFLSDSRDFIRQRDVFILESDTEPKDIYSHSGSSQPTIFTKSIPPQESGIAFYVDLHGHASKRGCFMYGNYFTEENDQVENMLYPKLISLNSANFDFLACNFSEKNMYAKDKRDGQSKEGSGRVAIHKATGIIHSYTLECNYNTGRCVNSIPAACHDCGRASPPPPPAFPPKYTTQVFEQIGRAVATAALDMAECNPWPRLIMSEYNNLTNLRAWMLKHLRNTKGVLPGTLKKKSTKSPVKASSLTSGSLSENSLIRTRSYSNSTASTNSQQNSPQIKPSINFTFLCSSSNHSPPKVSQRVLGPVRETKAQEKRRQQSLLRSSVRSPTACQQRLSTQAPSLSSGYPKTSSHAKTSCPLSLSLSMSGSGFSGLSQAAKVKNGTKKNNLEGDSTRQHIHQGHGIALLQNMQKRGSSHNNAEYSKSLESLGVRPSRIPVRRNGLLTNEKESPILRVWKYTTDTSLKHCSLADLAAVTSSLTVCSVPLLKSKAEEPVFICEATKETADQHFPAVSQDAAHLSAYQSVLSFCSEA |
| Enzyme Length | 944 |
| Uniprot Accession Number | B0JZV4 |
| Absorption | |
| Active Site | ACT_SITE 301; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00730 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:143622; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63796, Rhea:RHEA-COMP:16436, Rhea:RHEA-COMP:16437, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90782, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000250|UniProtKB:Q09M02}; |
| DNA Binding | |
| EC Number | 3.4.17.-; 3.4.17.24 |
| Enzyme Function | FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. {ECO:0000250|UniProtKB:Q09M02}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (2); Metal binding (3); Region (2) |
| Keywords | Carboxypeptidase;Cytoplasm;Cytoskeleton;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 105,600 |
| Kinetics | |
| Metal Binding | METAL 250; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 253; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 471; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | RHEA:60152; RHEA:60153; RHEA:60004; RHEA:60005; RHEA:63796; RHEA:63797; RHEA:63792; RHEA:63793 |
| Cross Reference Brenda |