| IED ID | IndEnz0002016125 |
| Enzyme Type ID | protease016125 |
| Protein Name |
Extracellular metalloproteinase mep EC 3.4.24.- AfuMep Allergen Asp f 5 Elastinolytic metalloproteinase mep Fungalysin mep allergen Asp f 5.0101 |
| Gene Name | mep AFUA_8G07080 |
| 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 | MRGLLLAGALALPASVFAHPAHQSYGLNRRTVDLNAFRLKSLAKYVNATETVIEAPSSFAPFKPQSYVEVATQHVKMIAPDATFRVVDDHYVGDNGVAHVHFRQTANGLDIDNADFNVNVGKDGKVFSYGNSFYTGQIPSSAALTKRDFSDPVTALKGTTNTLQLPITVDSASSESTEEKESYVFKGVSGTVSDPKAKLVYFVKDDGTLALAWRVETDIDSNWLLTYIDAKSGEEIHGVVDYVAEADYQVYAWGINDPTEGERTVIKDPWDSVASEFTWISDGSTNYTTSRGNNGIAQSNPSGGSSYLNNYRPSSSSLSFKYPYSVSSSPPSSYIDASIIQLFYTANIYHDLLYTLGFTEKAGNFEYNTNGQGGLGNDYVILNAQDGSGTNNANFATPPDGQPGRMRMYVWTESTPYRDGSFEAGIVIHEYTHGLSNRLTGGPANSNCLNALESGGMGEGWSDFMATAIRLKPGDKRSTDYTMGEWASNRAGGIRQYPYSTSLSTNPLTYTSVNSLNAVHAIGTVWASMLYEVLWNLIDKHGKNDAPKPTLRDGVPTDGKYLAMKLVMDGMALQPCNPNFVQARDAILDADTALTGGENQCEIWTAFAKRGLGAGAKYSSRNRVGSTEVPSGVC |
| Enzyme Length | 634 |
| Uniprot Accession Number | P46075 |
| Absorption | |
| Active Site | ACT_SITE 430; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by metalloprotease inhibitors EDTA, 1,10-phenanthroline, and phosphoramidon, but not by inhibitors specific for serine, cysteine, and aspartate proteases, such as PMSF, antipain, leupeptin, chymostatin, and pepstatin. Zn(2+) and, to a lesser extent, Co(2+) reversed the inhibition of 1,10-phenanthroline. {ECO:0000269|PubMed:8188335}. |
| Binding Site | |
| Calcium Binding | CA_BIND 375..378; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90"; CA_BIND 437..445; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90" |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor (By similarity). Catalyzes the hydrolysis of elastin (PubMed:7927676, PubMed:8188335). Hydrolyzes azocasein, synthetic fluorigenic substrate Abz-Ala-Ala-Phe-Phe-pNA, and His-Leu, Ala-Leu, Tyr-Leu, Gly-Phe, and Phe-Phe peptide bonds in the B chain of insulin (PubMed:8188335). {ECO:0000250, ECO:0000269|PubMed:7927676, ECO:0000269|PubMed:8188335}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius against azocasein. Retains 50% of the activity by incubation at 60 degrees Celsius for 1 hour. {ECO:0000269|PubMed:8188335}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:8188335}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (22); Calcium binding (2); Chain (1); Disulfide bond (2); Glycosylation (2); Helix (18); Metal binding (6); Mutagenesis (4); Natural variant (8); Propeptide (1); Sequence conflict (3); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Allergen;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Virulence;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: By Zn(2+) (PubMed:8188335). Expression is controlled by the prtT transcription factor (PubMed:19564390, PubMed:19564385). {ECO:0000269|PubMed:19564385, ECO:0000269|PubMed:19564390, ECO:0000269|PubMed:8188335}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24100314, ECO:0000269|PubMed:8188335}. Note=Secreted in the neutropenic mouse lungs by invading Aspergillus fumigatus. {ECO:0000269|PubMed:8188335}. |
| Modified Residue | |
| Post Translational Modification | PTM: Not glycosylated according to PubMed:8188335, but glycosylated according to PubMed:24100314. {ECO:0000269|PubMed:24100314, ECO:0000269|PubMed:8188335}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4K90; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,708 |
| Kinetics | |
| Metal Binding | METAL 245; /note="Zinc; via carbonyl oxygen; catalytic"; /evidence="ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90"; METAL 364; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90"; METAL 400; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90"; METAL 429; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90"; METAL 433; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90"; METAL 459; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:24100314, ECO:0007744|PDB:4K90" |
| Rhea ID | |
| Cross Reference Brenda |