| IED ID | IndEnz0002018883 | 
| Enzyme Type ID | protease018883 | 
| Protein Name | 
                        
                            
                                Flavastacin  EC 3.4.24.76  | 
                    
| Gene Name | |
| Organism | Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) | 
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Flavobacteriia Flavobacteriales Weeksellaceae Elizabethkingia Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) | 
| Enzyme Sequence | MTRKLLILSGCLILALNSCKSDMETTPASSVDHTTTQLNGTTIHKLLINGAYTYVNEVNGEYFYADDITITAEQFNQLKRMANPDISTVERSTIVSSFIKTWPNATVYYTLPSQGSLSTQAYNTFLTNINKAFDMISSKTSVKFVQRTNQTEYITFTYSTGNSSPLGWVKNRVNGIKIYNTTYPAIIAHEIMHSMGIMHEQCRPDRDQYIIVDTNRAQDGTRHNFNLYNDYAGHGEFDFGSVMMYKSTDFAIDPNLPVMTKLDGSTFGKQRDGLSAGDYAGINHLYGPVNSTSATNGTYTLTTSLAGDKNIDITGSSTADGTDVILYSATTGNNQKFIFRKSEHGYFTIKSILDSTKVLTVRNNGTANGTAVELRTNADTDAQKWLLFNLGNEGFGFAPKNAPSLRLEVKDGLTTNLTPIVIGSTDQTLQPYTKQRFTLTKVN | 
| Enzyme Length | 443 | 
| Uniprot Accession Number | Q47899 | 
| Absorption | |
| Active Site | ACT_SITE 190; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 | 
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolyzes polypeptides on the amino-side of Asp in -Xaa-|-Asp-. Acts very slowly on -Xaa-|-Glu.; EC=3.4.24.76; | 
| DNA Binding | |
| EC Number | 3.4.24.76 | 
| Enzyme Function | FUNCTION: Zinc metallendopeptidase that cleaves preferentially on N-terminal side of aspartate-containing substrates. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (2); Glycosylation (1); Metal binding (3); Propeptide (1); Signal peptide (1) | 
| Keywords | Direct protein sequencing;Glycoprotein;Hydrolase;Lectin;Metal-binding;Metalloprotease;Protease;Signal;Zinc;Zymogen | 
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: O-linked glycan consists of the Man, GlcNAc, GlcU, Glc, GlcU, Rha, Man heptasaccharide. {ECO:0000269|PubMed:7768917}. | 
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 | 
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 48,957 | 
| Kinetics | |
| Metal Binding | METAL 189; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 193; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 199; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 | 
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.76; |