| IED ID | IndEnz0010001606 |
| Enzyme Type ID | esterase001606 |
| Protein Name |
Probable cholinesterase EC 3.1.1.8 Acylcholine acylhydrolase |
| Gene Name | MIMI_L906 |
| Organism | Acanthamoeba polyphaga mimivirus (APMV) |
| Taxonomic Lineage | Viruses Varidnaviria Bamfordvirae Nucleocytoviricota Megaviricetes Imitervirales Mimiviridae Mimivirus Acanthamoeba polyphaga mimivirus (APMV) |
| Enzyme Sequence | MTDHKIIMLLLLGIYCIQATQFTQVNIDNGPIKGTLQYVEGRAIRVFKGIPFAEPPVNNLRWKAPVPYTKKWHNPLNTTEYKPKCPQYVAPGTVPEPRGISEDCLYTNVWAPVPEYHGETFPVMVWIHGGAFISGSPEDFGVGNFSILAVTKRIIIVAASYRVNAFGFFSSELLGKSQLEARGVYGLLDQRLGLKWVKNNIAAFGGKSKDITIYGQSAGGISVCLQAVTPLNDLPGEKLFTRVIGSSGYCDILPMTNNSADAGLVQKLNCTTKECLYALPWQNITNAVGPGFLSFQPTVGINKFLPDQPISLLADRTNPRSKNFVPDIYMQGFTANEGTFVLYNYFPQTYDNPNTPGFPTQQMADALSIASGNYSAEFYYNDLAPLYSTEYNSNVTYPGQGFISRVDDIMACNTRRNMIYWQQSKKTKAHSWYFDSAPDTHIYPSWTKVFHESDVFYVARRCDGLWCTNLTCQQDNLGKTMNIYWNSAIRAASLTPKNKMDNLRDVPVWPQYGKNEVVMHFTAVGENKGPQTSVLFSSIISADGDYQYLQRCKILDRVRAEYYNIPALDPETYLNACSK |
| Enzyme Length | 579 |
| Uniprot Accession Number | Q5UR02 |
| Absorption | |
| Active Site | ACT_SITE 217; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 337; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 451; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an acylcholine + H2O = a carboxylate + choline + H(+); Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8; |
| DNA Binding | |
| EC Number | 3.1.1.8 |
| Enzyme Function | FUNCTION: May be involved in the disruption of the host membrane. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (8); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Reference proteome;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 64,868 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21964 |
| Cross Reference Brenda |