| IED ID | IndEnz0002011896 |
| Enzyme Type ID | protease011896 |
| Protein Name |
Glutathione hydrolase-like YwrD proenzyme EC 2.3.2.2 Putative gamma-glutamyltransferase YwrD EC 3.4.19.13 Cleaved into: Glutathione hydrolase-like YwrD large chain; Glutathione hydrolase-like YwrD small chain |
| Gene Name | ywrD BSU36100 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MNKSVIGTKQMVVSPHYLASQAGNRILDKGGNAFDAAVAVSACLAVVYPHMTGLGGDSFWLTFHQETKAVKVYNGSGRSGKNVTRDVYKGKSAIPLRGIDSAITVPGMVDSWDAVLKEYGRLSLADVLEPARDYAQNGFPVSADQCRHTEKNIELLASTPYTADIFTRRGKAPVPGERFVQKELADSLNLIAEKGRSAFYEGDLAQRIVSHLQNNGSYMTIDDFKAHRGEWAAPVSSDYRGYSVYQAPPNSQGFTGLLTLNILENYDFTQIEHGSFEYYHVLVEALKKSFLDRDAVLTDPAFADIPLERLLDKRYAKQLAEEIGYLAIPAESRPVGSDTAYAAVIDADGNAVSFIQSLYFEFGSAVTAGDTGILLQNRGSFFSLDENHVNTLEPRKRTFHTLMPAMVCKGGKPKILYGTQGGEGQPQTQTAIITRMLDYGMHPQQAISEPRWVWGRTWGEEYEGLRVEGRFTDKTIQKLKDSGHLVEVVGDYDPLMGQAAAIKVDEEGFLQGGADPRGDGAAVGI |
| Enzyme Length | 525 |
| Uniprot Accession Number | O05218 |
| Absorption | |
| Active Site | ACT_SITE 339; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; |
| DNA Binding | |
| EC Number | 2.3.2.2; 3.4.19.13 |
| Enzyme Function | FUNCTION: Overexpressed protein with an N-terminal His tag has been reported not to hydrolyze glutathione; it is not clear if the construct is processed to 2 subunits (PubMed:14762019). {ECO:0000305|PubMed:14762019}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2) |
| Keywords | Acyltransferase;Hydrolase;Protease;Reference proteome;Transferase;Zymogen |
| Interact With | |
| Induction | INDUCTION: Positively regulated by TnrA under nitrogen-limited conditions. {ECO:0000269|PubMed:12823818}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,487 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23904; RHEA:28807; RHEA:59468 |
| Cross Reference Brenda |