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Protein

Diphtheria toxin

Gene
N/A
Organism
Corynephage beta
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

NAD+ + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2].

Activity regulationi

Partially inhibited by 1,8-naphthalimide (NAP).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei53NAD1
Binding sitei97NAD1
Active sitei1801
Sitei185Modification inactivates enzyme1

GO - Molecular functioni

Keywordsi

Molecular functionGlycosyltransferase, Toxin, Transferase
LigandNAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15583
ReactomeiR-HSA-5336415 Uptake and function of diphtheria toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Diphtheria toxin
Short name:
DT
Alternative name(s):
NAD(+)--diphthamide ADP-ribosyltransferase (EC:2.4.2.36)
Cleaved into the following 2 chains:
OrganismiCorynephage beta
Taxonomic identifieri10703 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdavirusunclassified Lambda-like viruses
Virus hostiCorynebacterium diphtheriae [TaxID: 1717]

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi180E → A: Loss of toxicity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 321 PublicationAdd BLAST32
ChainiPRO_000001934533 – 225Diphtheria toxin fragment AAdd BLAST193
ChainiPRO_0000019346226 – 567Diphtheria toxin fragment BAdd BLAST342

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi218 ↔ 233
Disulfide bondi493 ↔ 503

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PRIDEiP00588

Miscellaneous databases

PMAP-CutDBiP00588

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-15975409,EBI-15975409

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-60031N

Structurei

Secondary structure

1567
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP00588
SMRiP00588
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00588

Family & Domainsi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.490.40, 1 hit
2.60.40.700, 1 hit
InterProiView protein in InterPro
IPR036799 Diphtheria_tox_rcpt-bd_dom_sf
IPR036801 Diphtheria_tox_transloc_sf
IPR000512 Diphtheria_toxin
IPR022406 Diphtheria_toxin_catalytic_dom
IPR022404 Diphtheria_toxin_rcpt-bd_dom
IPR022405 Diphtheria_toxin_translocation
PfamiView protein in Pfam
PF02763 Diphtheria_C, 1 hit
PF01324 Diphtheria_R, 1 hit
PF02764 Diphtheria_T, 1 hit
PIRSFiPIRSF000490 Diphtheria_toxin, 1 hit
PRINTSiPR00769 DPTHRIATOXIN
SUPFAMiSSF49380 SSF49380, 1 hit
SSF56845 SSF56845, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00588-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLVRGYVVSR KLFASILIGA LLGIGAPPSA HAGADDVVDS SKSFVMENFS
60 70 80 90 100
SYHGTKPGYV DSIQKGIQKP KSGTQGNYDD DWKGFYSTDN KYDAAGYSVD
110 120 130 140 150
NENPLSGKAG GVVKVTYPGL TKVLALKVDN AETIKKELGL SLTEPLMEQV
160 170 180 190 200
GTEEFIKRFG DGASRVVLSL PFAEGSSSVE YINNWEQAKA LSVELEINFE
210 220 230 240 250
TRGKRGQDAM YEYMAQACAG NRVRRSVGSS LSCINLDWDV IRDKTKTKIE
260 270 280 290 300
SLKEHGPIKN KMSESPNKTV SEEKAKQYLE EFHQTALEHP ELSELKTVTG
310 320 330 340 350
TNPVFAGANY AAWAVNVAQV IDSETADNLE KTTAALSILP GIGSVMGIAD
360 370 380 390 400
GAVHHNTEEI VAQSIALSSL MVAQAIPLVG ELVDIGFAAY NFVESIINLF
410 420 430 440 450
QVVHNSYNRP AYSPGHKTQP FLHDGYAVSW NTVEDSIIRT GFQGESGHDI
460 470 480 490 500
KITAENTPLP IAGVLLPTIP GKLDVNKSKT HISVNGRKIR MRCRAIDGDV
510 520 530 540 550
TFCRPKSPVY VGNGVHANLH VAFHRSSSEK IHSNEISSDS IGVLGYQKTV
560
DHTKVNSKLS LFFEIKS
Length:567
Mass (Da):61,602
Last modified:May 1, 1991 - v2
Checksum:iCAF82A75EA693FF8
GO

Sequence cautioni

The sequence AAA32182 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti178 – 180SVE → VES AA sequence (PubMed:221484).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01722 Genomic DNA Translation: AAA32182.1 Different initiation.
X00703 Genomic DNA Translation: CAA25302.1

Similar proteinsi

Entry informationi

Entry nameiDTX_CORBE
AccessioniPrimary (citable) accession number: P00588
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 1, 1991
Last modified: September 12, 2018
This is version 115 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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