IED ID | IndEnz0002018483 |
Enzyme Type ID | protease018483 |
Protein Name |
Probable glutamate carboxypeptidase ARB_02390 EC 3.4.17.21 |
Gene Name | ARB_02390 |
Organism | Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Arthroderma benhamiae (Trichophyton mentagrophytes) Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
Enzyme Sequence | MIVKSLSLLALAAATVEGCVRERDVGSVDILSVLSKRGHGHPHLPHLSKYESMLINSFDNTTVDSWAYYYTHGIHIAGTNQSMAQWTADKWTEFGIPSSLVSYDVYLNYPVSHSLSLTHPDGTTWEASLVEDVLKEDDTTSYPDRIPTFHGYSASGEATAEYVYVGRGQKVDFERLIQLGVDLKGKIAIARYGGPFRGLKVKNAQDQGMIGCIIFTDPADDGNVTVANGLKAYPNGPARNPSAVQRGSVQFLSMFPGDPTTPGYPSRPDSPRKDKSPVVPKIPSIPISQLDAQPILAALDGHGTPGKEVNRTRWVGALNATYATGPAPGAKLSMSNVMRDTYTPIWNSIGIINGTEQDEVVIIGNHRDAWIIGGAGDPNSGSSIMVELAKAFGKLQKAGWKPKRTIVMCSWDAEEYGLVGSTEWVEEYLPWLKASAVAYLNIDVAVSGPVPDLSATPELHKLALESMKKVIWPYKGRQDTTMYDVWNTASGGEVGVLGSGSDYTAFVHNGIASLDTGAGGDGNTDPVYHYHSNYDSYHWMATYGDPGFHTHVAMGQFLGLLGYHLATDDIIPFDVTNYGVQMTKYLDVLKKYIAASKFPDLDVSKIESAICSFNVSANAVAKLQKKAEHNVHDQQLRKHLNTIYRDFGRGFVSQGGLPDREFYRHMLYAPGLDTGYAPTTFPGVTESLDAGNRTRAVEYIERASNAIYVAAGILSSCHDCNQFVAQE |
Enzyme Length | 727 |
Uniprot Accession Number | D4B1R0 |
Absorption | |
Active Site | ACT_SITE 414; /note=For NAALADase activity; /evidence=ECO:0000250|UniProtKB:Q04609; ACT_SITE 604; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 665; /note=Charge relay system; /evidence=ECO:0000255 |
Activity Regulation | |
Binding Site | BINDING 197; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04609; BINDING 530; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04609 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.; EC=3.4.17.21; Evidence={ECO:0000250|UniProtKB:Q04609}; |
DNA Binding | |
EC Number | 3.4.17.21 |
Enzyme Function | FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity (By similarity). Also exhibits a dipeptidyl-peptidase IV type activity (By similarity). {ECO:0000250|UniProtKB:Q04609}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Binding site (2); Chain (1); Domain (1); Glycosylation (8); Metal binding (8); Region (4); Signal peptide (1) |
Keywords | Carboxypeptidase;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460, ECO:0000269|PubMed:21919205}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 79,197 |
Kinetics | |
Metal Binding | METAL 261; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 264; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 366; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 415; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 423; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 426; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 443; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 531; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609 |
Rhea ID | |
Cross Reference Brenda |