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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].

Enzyme 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

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-60031N

Structurei

Secondary structure

1567
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi34 – 37Combined sources4
Helixi40 – 42Combined sources3
Beta strandi44 – 47Combined sources4
Beta strandi50 – 55Combined sources6
Turni57 – 61Combined sources5
Helixi62 – 65Combined sources4
Beta strandi71 – 73Combined sources3
Helixi80 – 82Combined sources3
Beta strandi84 – 89Combined sources6
Helixi91 – 95Combined sources5
Beta strandi101 – 103Combined sources3
Turni104 – 106Combined sources3
Beta strandi111 – 116Combined sources6
Beta strandi118 – 127Combined sources10
Helixi131 – 137Combined sources7
Beta strandi142 – 144Combined sources3
Helixi146 – 150Combined sources5
Helixi153 – 159Combined sources7
Beta strandi160 – 162Combined sources3
Beta strandi164 – 171Combined sources8
Beta strandi179 – 183Combined sources5
Helixi187 – 190Combined sources4
Beta strandi192 – 198Combined sources7
Helixi199 – 202Combined sources4
Helixi208 – 215Combined sources8
Helixi216 – 218Combined sources3
Helixi238 – 253Combined sources16
Helixi256 – 263Combined sources8
Helixi272 – 286Combined sources15
Helixi290 – 292Combined sources3
Helixi293 – 299Combined sources7
Helixi303 – 305Combined sources3
Helixi307 – 320Combined sources14
Helixi323 – 326Combined sources4
Helixi329 – 336Combined sources8
Helixi342 – 346Combined sources5
Helixi358 – 379Combined sources22
Turni387 – 390Combined sources4
Helixi391 – 407Combined sources17
Beta strandi421 – 423Combined sources3
Beta strandi426 – 432Combined sources7
Helixi433 – 436Combined sources4
Beta strandi437 – 439Combined sources3
Beta strandi444 – 457Combined sources14
Beta strandi459 – 461Combined sources3
Beta strandi463 – 467Combined sources5
Turni470 – 472Combined sources3
Beta strandi473 – 475Combined sources3
Turni477 – 479Combined sources3
Beta strandi481 – 484Combined sources4
Beta strandi487 – 489Combined sources3
Beta strandi491 – 496Combined sources6
Turni497 – 499Combined sources3
Beta strandi500 – 507Combined sources8
Beta strandi509 – 512Combined sources4
Beta strandi517 – 525Combined sources9
Turni533 – 535Combined sources3
Beta strandi540 – 550Combined sources11
Beta strandi553 – 562Combined sources10
Beta strandi564 – 566Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DDTX-ray2.00A33-567[»]
1DTPX-ray2.50A33-222[»]
1F0LX-ray1.55A/B33-567[»]
1MDTX-ray2.30A/B33-567[»]
1SGKX-ray2.30A33-567[»]
1TOXX-ray2.30A/B33-567[»]
1XDTX-ray2.65T33-567[»]
4AE0X-ray2.00A33-567[»]
4AE1X-ray2.08A/B33-567[»]
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: May 23, 2018
This is version 114 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

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