Detail Information for IndEnz0010000642
IED ID IndEnz0010000642
Enzyme Type ID esterase000642
Protein Name Hemagglutinin-esterase
HE protein
EC 3.1.1.53
E3 glycoprotein
Gene Name HE
Organism Breda virus 1 (BRV-1)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Tornidovirineae Tobaniviridae Torovirinae Torovirus Renitovirus Bovine torovirus Breda virus Breda virus 1 (BRV-1)
Enzyme Sequence MLSLILFFPSFAFAATPVTPYYGPGHITFDWCGFGDSRSDCTNPQSPMSLDIPQQLCPKFSSKSSSSMFLSLHWNNHSSFVSYDYFNCGVEKVFYEGVNFSPRKQYSCWDEGVDGWIELKTRFYTKLYQMATTSRCIKLIQLQAPSSLPTLQAGVCRTNKQLPDNPRLALLSDTVPTSVQFVLPGSSGTTICTKHLVPFCYLNHGCFTTGGSCLPFGVSYVSDSFYYGYYDATPQIGSTESHDYVCDYLFMEPGTYNASTVGKFLVYPTKSYCMDTMNITVPVQAVQSIWSEQYASDDAIGQACKAPYCIFYNKTTPYTVTNGSDANHGDDEVRMMMQGLLRNSSCISPQGSTPLALYSTEMIYEPNYGSCPQFYKLFDTSGNENIDVISSSYFVATWVLLVVVVILIFVIISFFC
Enzyme Length 416
Uniprot Accession Number P0C0V9
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; Evidence={ECO:0000269|PubMed:19721004}; 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:0000269|PubMed:19721004};
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. {ECO:0000269|PubMed:19721004}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (28); Chain (1); Disulfide bond (6); Glycosylation (6); Helix (9); Mutagenesis (6); Natural variant (10); Region (3); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2)
Keywords 3D-structure;Disulfide bond;Glycoprotein;Hemagglutinin;Host cell membrane;Host membrane;Hydrolase;Membrane;Reference proteome;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
Signal Peptide SIGNAL 1..14; /evidence=ECO:0000255
Structure 3D X-ray crystallography (2)
Cross Reference PDB 3I26; 3I27;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 46,440
Kinetics
Metal Binding
Rhea ID RHEA:22600; RHEA:25564
Cross Reference Brenda