Detail Information for IndEnz0002000078
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