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Diphtheria toxin (DT) (NAD( )--diphthamide ADP-ribosyltransferase) (EC 2.4.2.36) [Cleaved into: Diphtheria toxin fragment A; Diphtheria toxin fragment B]

 DTX_CORBE               Reviewed;         567 AA.
P00588;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 2.
22-NOV-2017, entry version 113.
RecName: Full=Diphtheria toxin;
Short=DT;
AltName: Full=NAD(+)--diphthamide ADP-ribosyltransferase;
EC=2.4.2.36;
Contains:
RecName: Full=Diphtheria toxin fragment A;
Contains:
RecName: Full=Diphtheria toxin fragment B;
Flags: Precursor;
Corynephage beta.
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Siphoviridae;
Lambdavirus; unclassified Lambda-like viruses.
NCBI_TaxID=10703;
NCBI_TaxID=1717; Corynebacterium diphtheriae.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6316330; DOI=10.1073/pnas.80.22.6853;
Greenfield L., Bjorn M.J., Horn G., Fong D., Buck G.A., Collier R.J.,
Kaplan D.A.;
"Nucleotide sequence of the structural gene for diphtheria toxin
carried by corynebacteriophage beta.";
Proc. Natl. Acad. Sci. U.S.A. 80:6853-6857(1983).
[2]
PROTEIN SEQUENCE OF 33-225.
PubMed=221484;
Delange R.J., Williams L.C., Drazin R.E., Collier R.J.;
"The amino acid sequence of fragment A, an enzymically active fragment
of diphtheria toxin. III. The chymotryptic peptides, the peptides
derived by cleavage at tryptophan residues, and the complete sequence
of the protein.";
J. Biol. Chem. 254:5838-5842(1979).
[3]
ACTIVE SITE TRP-185.
PubMed=849463; DOI=10.1016/0005-2795(77)90064-2;
Michel A., Dirkx J.;
"Occurrence of tryptophan in the enzymically active site of diphtheria
toxin fragment A.";
Biochim. Biophys. Acta 491:286-295(1977).
[4]
ACTIVE SITE TYR-97.
PubMed=1990001;
Papini E., Santucci A., Schiavo G., Domenighini M., Neri P.,
Rappuoli R., Montecucco C.;
"Tyrosine 65 is photolabeled by 8-azidoadenine and 8-azidoadenosine at
the NAD binding site of diphtheria toxin.";
J. Biol. Chem. 266:2494-2498(1991).
[5]
FUNCTION AS AN ADP-RIBOSYLTRANSFERASE.
PubMed=18276581; DOI=10.1074/jbc.M710008200;
Jorgensen R., Purdy A.E., Fieldhouse R.J., Kimber M.S., Bartlett D.H.,
Merrill A.R.;
"Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae.";
J. Biol. Chem. 283:10671-10678(2008).
[6]
FUNCTION AS A TOXIN, FUNCTION AS AN ADP-RIBOSYLTRANSFERASE, ENZYME
REGULATION, EXPRESSION IN YEAST, AND MUTAGENESIS OF GLU-180.
PubMed=19793133; DOI=10.1111/j.1574-6968.2009.01777.x;
Turgeon Z., White D., Jorgensen R., Visschedyk D., Fieldhouse R.J.,
Mangroo D., Merrill A.R.;
"Yeast as a tool for characterizing mono-ADP-ribosyltransferase
toxins.";
FEMS Microbiol. Lett. 300:97-106(2009).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=1589020; DOI=10.1038/357216a0;
Choe S., Bennett M.J., Fujii G., Curmi P.M.G., Kantardjieff K.A.,
Collier R.J., Eisenberg D.;
"The crystal structure of diphtheria toxin.";
Nature 357:216-222(1992).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=8573568; DOI=10.1021/bi9520848;
Bell C.E., Eisenberg D.;
"Crystal structure of diphtheria toxin bound to nicotinamide adenine
dinucleotide.";
Biochemistry 35:1137-1149(1996).
[9]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=9012663; DOI=10.1021/bi962214s;
Bell C.E., Eisenberg D.;
"Crystal structure of nucleotide-free diphtheria toxin.";
Biochemistry 36:481-488(1997).
[10]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF COMPLEX WITH RECEPTOR.
PubMed=9659904; DOI=10.1016/S1097-2765(00)80008-8;
Louie G.V., Yang W., Bowman M.E., Choe S.;
"Crystal structure of the complex of diphtheria toxin with an
extracellular fragment of its receptor.";
Mol. Cell 1:67-78(1997).
-!- 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: NAD(+) + diphthamide-[translation elongation
factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-
[translation elongation factor 2].
-!- ENZYME REGULATION: Partially inhibited by 1,8-naphthalimide (NAP).
{ECO:0000269|PubMed:19793133}.
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15975409, EBI-15975409;
-!- SEQUENCE CAUTION:
Sequence=AAA32182.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; K01722; AAA32182.1; ALT_INIT; Genomic_DNA.
EMBL; X00703; CAA25302.1; -; Genomic_DNA.
PDB; 1DDT; X-ray; 2.00 A; A=33-567.
PDB; 1DTP; X-ray; 2.50 A; A=33-222.
PDB; 1F0L; X-ray; 1.55 A; A/B=33-567.
PDB; 1MDT; X-ray; 2.30 A; A/B=33-567.
PDB; 1SGK; X-ray; 2.30 A; A=33-567.
PDB; 1TOX; X-ray; 2.30 A; A/B=33-567.
PDB; 1XDT; X-ray; 2.65 A; T=33-567.
PDB; 4AE0; X-ray; 2.00 A; A=33-567.
PDB; 4AE1; X-ray; 2.08 A; A/B=33-567.
PDBsum; 1DDT; -.
PDBsum; 1DTP; -.
PDBsum; 1F0L; -.
PDBsum; 1MDT; -.
PDBsum; 1SGK; -.
PDBsum; 1TOX; -.
PDBsum; 1XDT; -.
PDBsum; 4AE0; -.
PDBsum; 4AE1; -.
ProteinModelPortal; P00588; -.
SMR; P00588; -.
DIP; DIP-60031N; -.
BioCyc; MetaCyc:MONOMER-15583; -.
Reactome; R-HSA-5336415; Uptake and function of diphtheria toxin.
EvolutionaryTrace; P00588; -.
PMAP-CutDB; P00588; -.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0047286; F:NAD+-diphthamide ADP-ribosyltransferase activity; EXP:Reactome.
GO; GO:0008320; F:protein transmembrane transporter activity; TAS:Reactome.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
Gene3D; 1.10.490.40; -; 1.
Gene3D; 2.60.40.700; -; 1.
InterPro; IPR036799; Diphtheria_tox_rcpt-bd_dom_sf.
InterPro; IPR036801; Diphtheria_tox_transloc_sf.
InterPro; IPR000512; Diphtheria_toxin.
InterPro; IPR022406; Diphtheria_toxin_catalytic_dom.
InterPro; IPR022404; Diphtheria_toxin_rcpt-bd_dom.
InterPro; IPR022405; Diphtheria_toxin_translocation.
Pfam; PF02763; Diphtheria_C; 1.
Pfam; PF01324; Diphtheria_R; 1.
Pfam; PF02764; Diphtheria_T; 1.
PIRSF; PIRSF000490; Diphtheria_toxin; 1.
PRINTS; PR00769; DPTHRIATOXIN.
SUPFAM; SSF49380; SSF49380; 1.
SUPFAM; SSF56845; SSF56845; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues;
Direct protein sequencing; Disulfide bond; Glycosyltransferase; NAD;
Signal; Toxin; Transferase.
SIGNAL 1 32 {ECO:0000269|PubMed:221484}.
CHAIN 33 225 Diphtheria toxin fragment A.
/FTId=PRO_0000019345.
CHAIN 226 567 Diphtheria toxin fragment B.
/FTId=PRO_0000019346.
ACT_SITE 180 180
BINDING 53 53 NAD.
BINDING 97 97 NAD.
SITE 185 185 Modification inactivates enzyme.
DISULFID 218 233
DISULFID 493 503
MUTAGEN 180 180 E->A: Loss of toxicity.
{ECO:0000269|PubMed:19793133}.
CONFLICT 178 180 SVE -> VES (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 34 37 {ECO:0000244|PDB:1F0L}.
HELIX 40 42 {ECO:0000244|PDB:1F0L}.
STRAND 44 47 {ECO:0000244|PDB:1F0L}.
STRAND 50 55 {ECO:0000244|PDB:1F0L}.
TURN 57 61 {ECO:0000244|PDB:1MDT}.
HELIX 62 65 {ECO:0000244|PDB:1F0L}.
STRAND 71 73 {ECO:0000244|PDB:1F0L}.
HELIX 80 82 {ECO:0000244|PDB:1F0L}.
STRAND 84 89 {ECO:0000244|PDB:1F0L}.
HELIX 91 95 {ECO:0000244|PDB:1F0L}.
STRAND 101 103 {ECO:0000244|PDB:1XDT}.
TURN 104 106 {ECO:0000244|PDB:1F0L}.
STRAND 111 116 {ECO:0000244|PDB:1F0L}.
STRAND 118 127 {ECO:0000244|PDB:1F0L}.
HELIX 131 137 {ECO:0000244|PDB:1F0L}.
STRAND 142 144 {ECO:0000244|PDB:4AE0}.
HELIX 146 150 {ECO:0000244|PDB:1F0L}.
HELIX 153 159 {ECO:0000244|PDB:1F0L}.
STRAND 160 162 {ECO:0000244|PDB:1DTP}.
STRAND 164 171 {ECO:0000244|PDB:1F0L}.
STRAND 179 183 {ECO:0000244|PDB:1F0L}.
HELIX 187 190 {ECO:0000244|PDB:1F0L}.
STRAND 192 198 {ECO:0000244|PDB:1F0L}.
HELIX 199 202 {ECO:0000244|PDB:1F0L}.
HELIX 208 215 {ECO:0000244|PDB:1F0L}.
HELIX 216 218 {ECO:0000244|PDB:1F0L}.
HELIX 238 253 {ECO:0000244|PDB:1F0L}.
HELIX 256 263 {ECO:0000244|PDB:1F0L}.
HELIX 272 286 {ECO:0000244|PDB:1F0L}.
HELIX 290 292 {ECO:0000244|PDB:1F0L}.
HELIX 293 299 {ECO:0000244|PDB:1F0L}.
HELIX 303 305 {ECO:0000244|PDB:1F0L}.
HELIX 307 320 {ECO:0000244|PDB:1F0L}.
HELIX 323 326 {ECO:0000244|PDB:1F0L}.
HELIX 329 336 {ECO:0000244|PDB:1F0L}.
HELIX 342 346 {ECO:0000244|PDB:1F0L}.
HELIX 358 379 {ECO:0000244|PDB:1F0L}.
TURN 387 390 {ECO:0000244|PDB:1F0L}.
HELIX 391 407 {ECO:0000244|PDB:1F0L}.
STRAND 421 423 {ECO:0000244|PDB:1F0L}.
STRAND 426 432 {ECO:0000244|PDB:1F0L}.
HELIX 433 436 {ECO:0000244|PDB:1F0L}.
STRAND 437 439 {ECO:0000244|PDB:1F0L}.
STRAND 444 457 {ECO:0000244|PDB:1F0L}.
STRAND 459 461 {ECO:0000244|PDB:1F0L}.
STRAND 463 467 {ECO:0000244|PDB:1F0L}.
TURN 470 472 {ECO:0000244|PDB:1F0L}.
STRAND 473 475 {ECO:0000244|PDB:1F0L}.
TURN 477 479 {ECO:0000244|PDB:1F0L}.
STRAND 481 484 {ECO:0000244|PDB:1F0L}.
STRAND 487 489 {ECO:0000244|PDB:1F0L}.
STRAND 491 496 {ECO:0000244|PDB:1F0L}.
TURN 497 499 {ECO:0000244|PDB:1F0L}.
STRAND 500 507 {ECO:0000244|PDB:1F0L}.
STRAND 509 512 {ECO:0000244|PDB:1F0L}.
STRAND 517 525 {ECO:0000244|PDB:1F0L}.
TURN 533 535 {ECO:0000244|PDB:1F0L}.
STRAND 540 550 {ECO:0000244|PDB:1F0L}.
STRAND 553 562 {ECO:0000244|PDB:1F0L}.
STRAND 564 566 {ECO:0000244|PDB:1F0L}.
SEQUENCE 567 AA; 61602 MW; CAF82A75EA693FF8 CRC64;
MLVRGYVVSR KLFASILIGA LLGIGAPPSA HAGADDVVDS SKSFVMENFS SYHGTKPGYV
DSIQKGIQKP KSGTQGNYDD DWKGFYSTDN KYDAAGYSVD NENPLSGKAG GVVKVTYPGL
TKVLALKVDN AETIKKELGL SLTEPLMEQV GTEEFIKRFG DGASRVVLSL PFAEGSSSVE
YINNWEQAKA LSVELEINFE TRGKRGQDAM YEYMAQACAG NRVRRSVGSS LSCINLDWDV
IRDKTKTKIE SLKEHGPIKN KMSESPNKTV SEEKAKQYLE EFHQTALEHP ELSELKTVTG
TNPVFAGANY AAWAVNVAQV IDSETADNLE KTTAALSILP GIGSVMGIAD GAVHHNTEEI
VAQSIALSSL MVAQAIPLVG ELVDIGFAAY NFVESIINLF QVVHNSYNRP AYSPGHKTQP
FLHDGYAVSW NTVEDSIIRT GFQGESGHDI KITAENTPLP IAGVLLPTIP GKLDVNKSKT
HISVNGRKIR MRCRAIDGDV TFCRPKSPVY VGNGVHANLH VAFHRSSSEK IHSNEISSDS
IGVLGYQKTV DHTKVNSKLS LFFEIKS


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