Detail Information for IndEnz0010001053
IED ID IndEnz0010001053
Enzyme Type ID esterase001053
Protein Name Hemagglutinin-esterase
HE protein
EC 3.1.1.53
E3 glycoprotein
Gene Name HE 2b
Organism Murine coronavirus (strain S) (MHV-S) (Murine hepatitis virus)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Betacoronavirus Embecovirus Murine coronavirus Murine hepatitis virus Murine coronavirus (strain S) (MHV-S) (Murine hepatitis virus)
Enzyme Sequence MGCMCIAMAPRTLLLLIGCQLVFGFNEPLNIVSHLNDDWFLFGDSRSDCTYVENNGHPKLDWLDLDPKLCNSGRISAKSGNSLFRSFHFIDFYNYSGEGDQVIFYEGVNFSPSHGFKCLAYGDNKRWMGNKARFYARVYEKMAQYRSLSFVNVSYAYGGNAKPTSICKDKTLTLNNPTFISKESNYVDYYYESEANFTLQGCDEFIVPLCVFNGHSKGSSSDPANKYYTDSQSYYNMDTGVLYGFNSTLDVGNTVQNPGLDLTCRYLALTPGNYKAVSLEYLLSLPSKAICLRKPKSFMPVQVVDSRWNSTRQSDNMTAVACQLPYCFFRNTSADYSGGTHDVHHGDFHFRQLLSGLLYNVSCIAQQGAFVYNNVSSSWPAYGYGHCPTAANIGYMAPVCIYDPLPVILLGVLLGIAVLIIVFLMFYFMTDSGVRLHEA
Enzyme Length 439
Uniprot Accession Number P31614
Absorption
Active Site ACT_SITE 45; /note="Nucleophile"; /evidence="ECO:0000255|HAMAP-Rule:MF_04207, ECO:0000269|PubMed:22291594"; ACT_SITE 342; /note="Charge relay system"; /evidence="ECO:0000255|HAMAP-Rule:MF_04207, ECO:0000269|PubMed:22291594"; ACT_SITE 345; /note="Charge relay system"; /evidence="ECO:0000255|HAMAP-Rule:MF_04207, ECO:0000269|PubMed:22291594"
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, ECO:0000269|PubMed:22291594}; 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, ECO:0000269|PubMed:22291594};
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, ECO:0000269|PubMed:22291594}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (26); Chain (1); Disulfide bond (7); Glycosylation (9); Helix (5); Mutagenesis (6); Region (3); Sequence conflict (6); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5)
Keywords 3D-structure;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, ECO:0000269|PubMed:22291594}.
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255|HAMAP-Rule:MF_04207
Structure 3D X-ray crystallography (2)
Cross Reference PDB 4C7L; 4C7W;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 49,205
Kinetics
Metal Binding
Rhea ID RHEA:22600; RHEA:25564
Cross Reference Brenda