| IED ID | IndEnz0002016463 |
| Enzyme Type ID | protease016463 |
| Protein Name |
Cys-Gly metallodipeptidase DUG1 EC 3.4.13.- Deficient in utilization of glutathione protein 1 GSH degradosomal complex subunit DUG1 |
| Gene Name | DUG1 YFR044C |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFHDIKMVDLGIQPPPISTPNLSLPPVILSRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEAKGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDELIKKEANGYFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQVLGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTSLYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPAKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLNSPNKCRTELIHDGAYWVSDPFNAQFTAAKKATKLVYGVDPDFTREGGSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQYYSESPEN |
| Enzyme Length | 481 |
| Uniprot Accession Number | P43616 |
| Absorption | |
| Active Site | ACT_SITE 104; /evidence=ECO:0000250; ACT_SITE 171; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.13.- |
| Enzyme Function | FUNCTION: Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2-DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides. {ECO:0000269|PubMed:17179087, ECO:0000269|PubMed:19346245}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (19); Chain (1); Helix (17); Metal binding (6); Modified residue (1); Turn (7) |
| Keywords | 3D-structure;Cytoplasm;Dipeptidase;Hydrolase;Manganese;Metal-binding;Metalloprotease;Mitochondrion;Phosphoprotein;Protease;Reference proteome;Zinc |
| Interact With | Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17179087}. Mitochondrion {ECO:0000269|PubMed:16823961}. |
| Modified Residue | MOD_RES 451; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4G1P; |
| Mapped Pubmed ID | 11805826; 11805837; 14690591; 16361226; 16429126; 16554755; 19119416; 19536198; 20868722; 21771575; 22034500; 22170048; 22277648; 23198979; 24040173; 25427234; 26227410; 27163342; 29636254; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,871 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 mM for Cys-Gly (at pH 8.0 and in the presence of 20 uM manganese ions); KM=0.8 mM for Cys-Gly (at pH 8.0 and in the presence of 200 uM zinc ions); |
| Metal Binding | METAL 102; /note=Zinc 2; /evidence=ECO:0000250; METAL 137; /note=Zinc 1; /evidence=ECO:0000250; METAL 137; /note=Zinc 2; /evidence=ECO:0000250; METAL 172; /note=Zinc 1; /evidence=ECO:0000250; METAL 200; /note=Zinc 2; /evidence=ECO:0000250; METAL 450; /note=Zinc 1; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |