| IED ID | IndEnz0010001054 |
| Enzyme Type ID | esterase001054 |
| Protein Name |
Hemagglutinin-esterase HE protein EC 3.1.1.53 E3 glycoprotein |
| Gene Name | HE |
| Organism | Breda virus 2 (BRV-2) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Tornidovirineae Tobaniviridae Torovirinae Torovirus Renitovirus Bovine torovirus Breda virus Breda virus 2 (BRV-2) |
| Enzyme Sequence | MLSLILFFPSFAFAATPVTPYYGPGHITFDWCGFGDSRSDCTNPQSPMSLDIPQQLCPKFSSKSSSSMFLSLHWNNHSSFVSYDYFNCGVEKVFYEGVNFSPRKQYSCWDEGVDGWIELKTRFYTKLYQMATTSRCIKLIQLQAPSSLPTLQAGVCRTNKQLPDNPRLALLSDTVPTSVQFVLPGSSGTTICTKHLVPFCYLNHGCFTTGGSCLPFGVSYVSDSFYYGYYDATPQIGSTESHDYVCDYLFMEPGTYNASTVGKFLVYPTKSYCMDTMNITVPVQAVQSIWSEQYASDDAIGQACKAPYCIFYNKTTPYTVTNGSDANHGDDEVRMMMQGLLRNSSCISPQGSTPLALYSTEMIYEPNYGSCPQFYKLFDTSGNENIDVISSSYFVATWVLLVVVVILIFVIISFFC |
| Enzyme Length | 416 |
| Uniprot Accession Number | P0C0W0 |
| Absorption | |
| Active Site | ACT_SITE 37; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 325; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 328; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-acetylneuraminate; Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089, ChEBI:CHEBI:35418; EC=3.1.1.53; CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-4-O-acetylneuraminate = acetate + H(+) + N-acetylneuraminate; Xref=Rhea:RHEA:25564, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29006, ChEBI:CHEBI:30089, ChEBI:CHEBI:35418; EC=3.1.1.53; |
| DNA Binding | |
| EC Number | 3.1.1.53 |
| Enzyme Function | FUNCTION: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-9-di-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. Also hydrolyzes 5-N-acetyl-4-O-acetylneuraminic acid and N-acetyl-9-O-acetylneuraminic acid, but displays a substrate preference for N-acetyl-9-di-O-acetylneuraminic acid. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture. However, its presence in the virus may alter its pathogenicity. May become a target for both the humoral and the cellular branches of the immune system. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Glycosylation (6); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Disulfide bond;Glycoprotein;Hemagglutinin;Host cell membrane;Host membrane;Hydrolase;Membrane;Signal;Transmembrane;Transmembrane helix;Viral envelope protein;Virion |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface (By similarity). {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000305}. |
| Signal Peptide | SIGNAL 1..14; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,440 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:22600; RHEA:25564 |
| Cross Reference Brenda |