Detail Information for IndEnz0010001642
IED ID IndEnz0010001642
Enzyme Type ID esterase001642
Protein Name S-formylglutathione hydrolase
FGH
EC 3.1.2.12
Gene Name YJL068C HRE299 J1102
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 MKVVKEFSVCGGRLIKLSHNSNSTKTSMNVNIYLPKHYYAQDFPRNKRIPTVFYLSGLTCTPDNASEKAFWQFQADKYGFAIVFPDTSPRGDEVANDPEGSWDFGQGAGFYLNATQEPYAQHYQMYDYIHKELPQTLDSHFNKNGDVKLDFLDNVAITGHSMGGYGAICGYLKGYSGKRYKSCSAFAPIVNPSNVPWGQKAFKGYLGEEKAQWEAYDPCLLIKNIRHVGDDRILIHVGDSDPFLEEHLKPELLLEAVKATSWQDYVEIKKVHGFDHSYYFVSTFVPEHAEFHARNLGLI
Enzyme Length 299
Uniprot Accession Number P40363
Absorption
Active Site ACT_SITE 161; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P10768; ACT_SITE 241; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P10768; ACT_SITE 276; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P10768
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H2O + S-formylglutathione = formate + glutathione + H(+); Xref=Rhea:RHEA:14961, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:57688, ChEBI:CHEBI:57925; EC=3.1.2.12; Evidence={ECO:0000269|PubMed:10427036};
DNA Binding
EC Number 3.1.2.12
Enzyme Function FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. {ECO:0000269|PubMed:10427036}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:10427036};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:10427036};
Pathway
nucleotide Binding
Features Active site (3); Beta strand (10); Chain (1); Helix (16); Metal binding (2); Turn (2)
Keywords 3D-structure;Copper;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Reference proteome;Serine esterase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10427036}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (4)
Cross Reference PDB 1PV1; 3C6B; 4FLM; 4FOL;
Mapped Pubmed ID 10509023; 19854949; 26760759; 27693354;
Motif
Gene Encoded By
Mass 33,934
Kinetics
Metal Binding METAL 1; /note="Copper; via amide nitrogen and carbonyl oxygen"; /evidence="ECO:0000269|PubMed:22906720, ECO:0007744|PDB:4FLM"; METAL 140; /note="Copper; via pros nitrogen"; /evidence="ECO:0000269|PubMed:22906720, ECO:0007744|PDB:4FLM"
Rhea ID RHEA:14961
Cross Reference Brenda 3.1.2.12;