Detail Information for IndEnz0002001488
IED ID IndEnz0002001488
Enzyme Type ID protease001488
Protein Name Dual function macrocyclase-peptidase POPB
EC 3.4.21.26
Prolyl oligopeptidase B
POP B
Toxin-processing prolyl oligopeptidase
Gene Name POPB GALMADRAFT_78538
Organism Galerina marginata (strain CBS 339.88)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Strophariaceae Galerina Galerina marginata Galerina marginata (strain CBS 339.88)
Enzyme Sequence MSSVTWAPGNYPSTRRSDHVDTYQSASKGEVPVPDPYQWLEESTDEVDKWTTAQADLAQSYLDQNADIQKLAEKFRASRNYAKFSAPTLLDDGHWYWFYNRGLQSQSVLYRSKEPALPDFSKGDDNVGDVFFDPNVLAADGSAGMVLCKFSPDGKFFAYAVSHLGGDYSTIYVRSTSSPLSQASVAQGVDGRLSDEVKWFKFSTIIWTKDSKGFLYQRYPARERHEGTRSDRNAMMCYHKVGTTQEEDIIVYQDNEHPEWIYGADTSEDGKYLYLYQFKDTSKKNLLWVAELDEDGVKSGIHWRKVVNEYAADYNIITNHGSLVYIKTNLNAPQYKVITIDLSKDEPEIRDFIPEEKDAKLAQVNCANEEYFVAIYKRNVKDEIYLYSKAGVQLTRLAPDFVGAASIANRQKQTHFFLTLSGFNTPGTIARYDFTAPETQRFSILRTTKVNELDPDDFESTQVWYESKDGTKIPMFIVRHKSTKFDGTAAAIQYGYGGFATSADPFFSPIILTFLQTYGAIFAVPSIRGGGEFGEEWHKGGRRETKVNTFDDFIAAAQFLVKNKYAAPGKVAINGASNGGLLVMGSIVRAPEGTFGAAVPEGGVADLLKFHKFTGGQAWISEYGNPSIPEEFDYIYPLSPVHNVRTDKVMPATLITVNIGDGRVVPMHSFKFIATLQHNVPQNPHPLLIKIDKSWLGHGMGKPTDKNVKDAADKWGFIARALGLELKTVE
Enzyme Length 730
Uniprot Accession Number H2E7Q8
Absorption
Active Site ACT_SITE 577; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:29051530"; ACT_SITE 661; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:29051530"; ACT_SITE 698; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:29051530"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000269|PubMed:28866879, ECO:0000269|PubMed:29051530};
DNA Binding
EC Number 3.4.21.26
Enzyme Function FUNCTION: Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate (PubMed:29051530). Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (PubMed:29051530). The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues (PubMed:28866879, PubMed:29051530). {ECO:0000269|PubMed:22202811, ECO:0000269|PubMed:28866879, ECO:0000269|PubMed:29051530}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (41); Chain (1); Compositional bias (1); Helix (22); Mutagenesis (5); Region (1); Turn (5)
Keywords 3D-structure;Hydrolase;Protease;Reference proteome;Serine protease
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (5)
Cross Reference PDB 5N4B; 5N4C; 5N4D; 5N4E; 5N4F;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 81,781
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23 uM for the full alpha-amanitin 35mer proprotein {ECO:0000269|PubMed:29051530}; KM=51 uM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=19 uM for the 25mer LWGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=8 uM for the 25mer IFGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=28 uM for the 25mer IWGIGSNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=10 uM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIS {ECO:0000269|PubMed:29051530}; KM=25 uM for the 19mer IWGIGCNPDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=380 uM for the 14mer IWGIGCNPWTAEHV {ECO:0000269|PubMed:29051530}; KM=24.4 uM for the 13mer IWGIGCNPWTAEH {ECO:0000269|PubMed:29051530};
Metal Binding
Rhea ID
Cross Reference Brenda