| IED ID | IndEnz0002000078 |
| Enzyme Type ID | protease000078 |
| Protein Name |
Pyruvate dehydrogenase acetyl-transferring-phosphatase 1, mitochondrial PDP 1 EC 3.1.3.43 Phosphatase two C protein 5 Protein phosphatase 2C homolog 5 PP2C-5 Protein phosphatase of PDH protein 1 Pyruvate dehydrogenase complex phosphatase 1 PDC phosphatase 1 |
| Gene Name | PTC5 PPP1 YOR090C YOR3157C |
| 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 | MSPLTRTVAIKKTVKVLSKCQSGREYTQKFLQRAYSTSHANSTYYSRTKLFISSHSKALNIALLSGSLLLTYSYYSPKKILSLDTINGIKDYSTNTSGNINMPSPNPKGTETQKSQRSQNDQSVLILNDSKIEAKLHDREESHFVNRGTGIFRYDVAQLPSNHPIEDDHVEQIITIPIESEDGKSIEKDLYFFGIFDGHGGPFTSEKLSKDLVRYVAYQLGQVYDQNKTVFHSDPNQLIDSAISKGFLKLDNDLVIESFRKLFQDPNNTNIANTLPAISGSCALLSLYNSTNSILKVAVTGDSRALICGLDNEGNWTVKSLSTDQTGDNLDEVRRIRKEHPGEPNVIRNGRILGSLQPSRAFGDYRYKIKEVDGKPLSDLPEVAKLYFRREPRDFKTPPYVTAEPVITSAKIGENTKFMVMGSDGLFELLTNEEIASLVIRWMDKNMNLAPVKAEPGKLPKVIDVSEDKEAQRPAFRYKDNNSSSPSGSNPEYLIEDKNVATHLIRNALSAGGRKEYVSALVSIPSPMSRRYRDDLTVTVAFFGDSGTPSIVSNATSIVMNPEATTKPKPRL |
| Enzyme Length | 572 |
| Uniprot Accession Number | Q12511 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] + phosphate; Xref=Rhea:RHEA:12669, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.43; Evidence={ECO:0000305|PubMed:18180296};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12670; Evidence={ECO:0000305|PubMed:18180296}; |
| DNA Binding | |
| EC Number | 3.1.3.43 |
| Enzyme Function | FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation of the E1 alpha subunit (PDA1) of the pyruvate dehydrogenase complex. {ECO:0000269|PubMed:16643908, ECO:0000269|PubMed:18180296}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Domain (1); Metal binding (5); Region (2); Transit peptide (1) |
| Keywords | Hydrolase;Magnesium;Manganese;Metal-binding;Mitochondrion;Protein phosphatase;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16643908, ECO:0000269|PubMed:22984289}. |
| Modified Residue | |
| Post Translational Modification | PTM: Processed by mitochondrial inner membrane protease (IMP) complex and released to the intermembrane space. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10572263; 10580002; 11805837; 15766533; 16554755; 19536198; 19753119; 19930686; 20489023; 21076010; 21606678; 24969434; 32398688; |
| Motif | |
| Gene Encoded By | |
| Mass | 63,669 |
| Kinetics | |
| Metal Binding | METAL 197; /note=Manganese 1; /evidence=ECO:0000250; METAL 197; /note=Manganese 2; /evidence=ECO:0000250; METAL 198; /note=Manganese 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 424; /note=Manganese 2; /evidence=ECO:0000250; METAL 480; /note=Manganese 2; /evidence=ECO:0000250 |
| Rhea ID | RHEA:12669; RHEA:12670 |
| Cross Reference Brenda |