UniProt functional annotation for P00588

UniProt code: P00588.

Organism: Corynephage beta.
Taxonomy: Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Siphoviridae; Lambdavirus; unclassified Lambdavirus.
 
Function: Diphtheria toxin, produced by a phage infecting Corynebacterium diphtheriae, is a proenzyme that, after activation, catalyzes the covalent attachment of the ADP ribose moiety of NAD to eukaryotic elongation factor 2 (eEF-2). Fragment A is the catalytic portion responsible for enzymatic ADP-ribosylation of elongation factor 2, while fragment B is responsible for binding of toxin to cell receptors and entry of fragment A. {ECO:0000269|PubMed:18276581, ECO:0000269|PubMed:19793133}.
 
Catalytic activity: Reaction=diphthamide-[translation elongation factor 2] + NAD(+) = H(+) + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] + nicotinamide; Xref=Rhea:RHEA:11820, Rhea:RHEA-COMP:10174, Rhea:RHEA- COMP:10175, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:82697; EC=2.4.2.36;
Activity regulation: Partially inhibited by 1,8-naphthalimide (NAP). {ECO:0000269|PubMed:19793133}.
Subunit: Homodimer.
Ptm: Proteolytic activation by host furin cleaves the protein in two parts, Diphtheria toxin fragment A and Diphtheria toxin fragment B; which remain associated via a disulfide bond. {ECO:0000269|PubMed:8253774}.
Sequence caution: Sequence=AAA32182.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.