| IED ID | IndEnz0002001635 |
| Enzyme Type ID | protease001635 |
| Protein Name |
Tripeptidyl-peptidase sed2 EC 3.4.14.10 Sedolisin-B |
| Gene Name | sed2 sedB AFUA_4G03490 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MFSSLLNRGALLAVVSLLSSSVAAEVFEKLSAVPQGWKYSHTPSDRDPIRLQIALKQHDVEGFETALLEMSDPYHPNYGKHFQTHEEMKRMLLPTQEAVESVRGWLESAGISDIEEDADWIKFRTTVGVANDLLDADFKWYVNEVGHVERLRTLAYSLPQSVASHVNMVQPTTRFGQIKPNRATMRGRPVQVDADILSAAVQAGDTSTCDQVITPQCLKDLYNIGDYKADPNGGSKVAFASFLEEYARYDDLAKFEEKLAPYAIGQNFSVIQYNGGLNDQNSASDSGEANLDLQYIVGVSSPIPVTEFSTGGRGLLIPDLSQPDPNDNSNEPYLEFLQNVLKMDQDKLPQVISTSYGEDEQTIPEKYARSVCNLYAQLGSRGVSVIFSSGDSGVGAACLTNDGTNRTHFPPQFPAACPWVTSVGGTTKTQPEEAVYFSSGGFSDLWERPSWQDSAVKRYLKKLGPRYKGLYNPKGRAFPDVAAQAENYAVFDKGVLHQFDGTSCSAPAFSAIVALLNDARLRAHKPVMGFLNPWLYSKASKGFNDIVKGGSKGCDGRNRFGGTPNGSPVVPYASWNATDGWDPATGLGTPDFGKLLSLAMRR |
| Enzyme Length | 602 |
| Uniprot Accession Number | Q70J59 |
| Absorption | |
| Active Site | ACT_SITE 288; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 292; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 503; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide.; EC=3.4.14.10; |
| DNA Binding | |
| EC Number | 3.4.14.10 |
| Enzyme Function | FUNCTION: Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence. {ECO:0000269|PubMed:16517617}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 6. {ECO:0000269|PubMed:16517617}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Glycosylation (3); Metal binding (4); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:16517617}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:16517617}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 65,839 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=62.5 uM for Phe-Pro-Ala-pNA (at 20 degrees Celsius) {ECO:0000269|PubMed:16517617}; |
| Metal Binding | METAL 545; /note=Calcium; /evidence=ECO:0000250; METAL 546; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 580; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 582; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.9; |