| IED ID | IndEnz0010001291 |
| Enzyme Type ID | esterase001291 |
| Protein Name |
Hemagglutinin-esterase HE protein EC 3.1.1.53 E3 glycoprotein |
| Gene Name | HE 2b |
| Organism | Bovine coronavirus (strain F15) (BCoV) (BCV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Betacoronavirus Embecovirus Betacoronavirus 1 Bovine coronavirus Bovine coronavirus (strain F15) (BCoV) (BCV) |
| Enzyme Sequence | MFLLPRFILVSCIIGSLGFDNPPTNVVSHLNGDWFLFGDSRSDCNHVVNTNPRNYSYMDLNPALCDSGKISSKAGNSIFRSFHFTDFYNYTGEGQQIIFYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIAREANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGNYLAISNELLLTVPTKAICLNKRKDFTPVQVVHSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSILSGLLYDSPCFSQQGVFRYNNVSSVWPLYPYGRCPTAADINTPDVPICVYDPLPLILLGILLGVAVIIIVVLLLYFMVENGTRL |
| Enzyme Length | 421 |
| Uniprot Accession Number | P33468 |
| Absorption | |
| Active Site | ACT_SITE 40; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_04207; ACT_SITE 326; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_04207; ACT_SITE 329; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_04207 |
| 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; Evidence={ECO:0000255|HAMAP-Rule:MF_04207}; 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; Evidence={ECO:0000255|HAMAP-Rule:MF_04207}; |
| 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-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. 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. May become a target for both the humoral and the cellular branches of the immune system. {ECO:0000255|HAMAP-Rule:MF_04207}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Glycosylation (8); 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:0000255|HAMAP-Rule:MF_04207}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04207}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04207}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04207}. 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. {ECO:0000255|HAMAP-Rule:MF_04207}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated in the host RER. {ECO:0000255|HAMAP-Rule:MF_04207}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255|HAMAP-Rule:MF_04207 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,415 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:22600; RHEA:25564 |
| Cross Reference Brenda |