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Botulinum neurotoxin type D (BoNT/D) (EC 3.4.24.69) (Bontoxilysin-D) [Cleaved into: Botulinum neurotoxin D light chain; Botulinum neurotoxin D heavy chain]

 BXD_CLOBO               Reviewed;        1276 AA.
P19321;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
23-MAY-2018, entry version 157.
RecName: Full=Botulinum neurotoxin type D;
Short=BoNT/D;
EC=3.4.24.69;
AltName: Full=Bontoxilysin-D;
Contains:
RecName: Full=Botulinum neurotoxin D light chain;
Contains:
RecName: Full=Botulinum neurotoxin D heavy chain;
Flags: Precursor;
Name=botD;
Clostridium botulinum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1491;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BVD/-3 / Type D;
PubMed=2216736; DOI=10.1093/nar/18.18.5556;
Binz T., Kurazono H., Popoff M.R., Eklund M.W., Sakaguchi G.,
Kozaki S., Krieglstein K., Henschen A., Gill D.M., Niemann H.;
"Nucleotide sequence of the gene encoding Clostridium botulinum
neurotoxin type D.";
Nucleic Acids Res. 18:5556-5556(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CB-16 / Type D;
PubMed=1420572; DOI=10.1292/jvms.54.905;
Sunagawa H., Ohyama T., Watanabe T., Inoue K.;
"The complete amino acid sequence of the Clostridium botulinum type D
neurotoxin, deduced by nucleotide sequence analysis of the encoding
phage d-16 phi genome.";
J. Vet. Med. Sci. 54:905-913(1992).
[3]
PARTIAL PROTEIN SEQUENCE.
STRAIN=D-1873 / Type D, and South African / Type D;
PubMed=2668193;
Moriishi K., Syuto B., Kubo S., Oguma K.;
"Molecular diversity of neurotoxins from Clostridium botulinum type D
strains.";
Infect. Immun. 57:2886-2891(1989).
[4]
IDENTIFICATION OF SUBSTRATE.
PubMed=8175689;
Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F.,
Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H.;
"Cleavage of members of the synaptobrevin/VAMP family by types D and F
botulinal neurotoxins and tetanus toxin.";
J. Biol. Chem. 269:12764-12772(1994).
[5]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-436 IN COMPLEX WITH ZINC
IONS.
PubMed=16519520; DOI=10.1021/bi052518r;
Arndt J.W., Chai Q., Christian T., Stevens R.C.;
"Structure of botulinum neurotoxin type D light chain at 1.65 A
resolution: repercussions for VAMP-2 substrate specificity.";
Biochemistry 45:3255-3262(2006).
-!- FUNCTION: Botulinum toxin acts by inhibiting neurotransmitter
release. It binds to peripheral neuronal synapses, is internalized
and moves by retrograde transport up the axon into the spinal cord
where it can move between postsynaptic and presynaptic neurons. It
inhibits neurotransmitter release by acting as a zinc
endopeptidase that cleaves the '60-Lys-|-Leu-61' bond of
synaptobrevins-1 and -2.
-!- CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the
neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No
detected action on small molecule substrates.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Disulfide-linked heterodimer of a light chain (L) and a
heavy chain (H). The light chain has the pharmacological activity,
while the N- and C-terminal of the heavy chain mediate channel
formation and toxin binding, respectively.
{ECO:0000269|PubMed:16519520}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin D light chain:
Secreted. Host cytoplasm, host cytosol.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin D heavy chain:
Secreted. Host cell junction, host synapse, host presynaptic cell
membrane {ECO:0000305}.
-!- MISCELLANEOUS: There are seven antigenically distinct forms of
botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
-!- MISCELLANEOUS: Botulinum type D neurotoxin is synthesized by D
strains of C.botulinum which carry the appropriate bacteriophage.
-!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial
Neurotoxins;
URL="https://botdb.abcc.ncifcrf.gov/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X54254; CAA38175.1; -; Genomic_DNA.
EMBL; S49407; AAB24244.1; -; Genomic_DNA.
PIR; S11455; S11455.
PDB; 2FPQ; X-ray; 1.65 A; A=1-436.
PDB; 3N7J; X-ray; 2.00 A; A=862-1276.
PDB; 3OBR; X-ray; 1.72 A; A=863-1276.
PDB; 3OBT; X-ray; 2.00 A; A=863-1276.
PDB; 3OGG; X-ray; 1.65 A; A=863-1276.
PDB; 3RMX; X-ray; 2.75 A; A/B/C/D=862-1276.
PDB; 3RMY; X-ray; 2.30 A; A/B/C/D=862-1276.
PDB; 5BQM; X-ray; 3.10 A; A/C=1-437, B/D=450-861.
PDB; 5BQN; X-ray; 2.30 A; A=1-437, A=450-862.
PDBsum; 2FPQ; -.
PDBsum; 3N7J; -.
PDBsum; 3OBR; -.
PDBsum; 3OBT; -.
PDBsum; 3OGG; -.
PDBsum; 3RMX; -.
PDBsum; 3RMY; -.
PDBsum; 5BQM; -.
PDBsum; 5BQN; -.
ProteinModelPortal; P19321; -.
SMR; P19321; -.
PRIDE; P19321; -.
BRENDA; 3.4.24.69; 1462.
Reactome; R-HSA-5250955; Toxicity of botulinum toxin type D (BoNT/D).
EvolutionaryTrace; P19321; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
GO; GO:0044156; C:host cell junction; IEA:UniProtKB-KW.
GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome.
GO; GO:0008320; F:protein transmembrane transporter activity; TAS:Reactome.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0051609; P:inhibition of neurotransmitter uptake; IEA:InterPro.
Gene3D; 1.20.1120.10; -; 2.
InterPro; IPR000395; Bot/tetX_LC.
InterPro; IPR036248; Clostridium_toxin_transloc.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
InterPro; IPR013104; Toxin_rcpt-bd_C.
InterPro; IPR012928; Toxin_rcpt-bd_N.
InterPro; IPR012500; Toxin_trans.
Pfam; PF01742; Peptidase_M27; 1.
Pfam; PF07951; Toxin_R_bind_C; 1.
Pfam; PF07953; Toxin_R_bind_N; 1.
Pfam; PF07952; Toxin_trans; 1.
PRINTS; PR00760; BONTOXILYSIN.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF50386; SSF50386; 2.
SUPFAM; SSF58091; SSF58091; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Host cell junction; Host cell membrane; Host cytoplasm; Host membrane;
Host synapse; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Neurotoxin; Protease; Secreted; Toxin; Transmembrane; Virulence; Zinc.
CHAIN 1 442 Botulinum neurotoxin D light chain.
/FTId=PRO_0000029219.
CHAIN 443 1276 Botulinum neurotoxin D heavy chain.
/FTId=PRO_0000029220.
ACT_SITE 230 230 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 229 229 Zinc; catalytic.
METAL 233 233 Zinc; catalytic.
METAL 269 269 Zinc; catalytic.
DISULFID 437 450 Interchain (between light and heavy
chains). {ECO:0000305}.
VARIANT 15 16 ND -> PV (in strain: D-SA).
VARIANT 17 18 ND -> LQ (in strain: D-1873).
VARIANT 452 452 K -> Q (in strain: D-SA).
VARIANT 457 457 R -> F (in strain: D-1873).
VARIANT 457 457 R -> T (in strain: D-SA).
VARIANT 462 462 A -> D (in strain: D-1873).
VARIANT 489 489 K -> N (in strain: CB16).
VARIANT 644 644 N -> K (in strain: CB16).
VARIANT 1122 1122 Q -> R (in strain: CB16).
STRAND 16 23 {ECO:0000244|PDB:2FPQ}.
STRAND 34 40 {ECO:0000244|PDB:2FPQ}.
STRAND 43 46 {ECO:0000244|PDB:2FPQ}.
STRAND 53 55 {ECO:0000244|PDB:5BQM}.
TURN 67 69 {ECO:0000244|PDB:2FPQ}.
TURN 74 77 {ECO:0000244|PDB:2FPQ}.
HELIX 80 97 {ECO:0000244|PDB:2FPQ}.
HELIX 101 112 {ECO:0000244|PDB:2FPQ}.
STRAND 120 122 {ECO:0000244|PDB:5BQM}.
STRAND 126 128 {ECO:0000244|PDB:2FPQ}.
TURN 132 134 {ECO:0000244|PDB:2FPQ}.
STRAND 136 142 {ECO:0000244|PDB:2FPQ}.
STRAND 145 152 {ECO:0000244|PDB:2FPQ}.
STRAND 155 159 {ECO:0000244|PDB:2FPQ}.
HELIX 169 172 {ECO:0000244|PDB:5BQM}.
HELIX 181 183 {ECO:0000244|PDB:2FPQ}.
STRAND 184 186 {ECO:0000244|PDB:2FPQ}.
STRAND 190 193 {ECO:0000244|PDB:2FPQ}.
STRAND 201 203 {ECO:0000244|PDB:2FPQ}.
TURN 212 214 {ECO:0000244|PDB:5BQM}.
STRAND 218 220 {ECO:0000244|PDB:2FPQ}.
HELIX 223 238 {ECO:0000244|PDB:2FPQ}.
STRAND 247 249 {ECO:0000244|PDB:5BQM}.
HELIX 267 273 {ECO:0000244|PDB:2FPQ}.
HELIX 275 280 {ECO:0000244|PDB:2FPQ}.
HELIX 283 306 {ECO:0000244|PDB:2FPQ}.
STRAND 309 312 {ECO:0000244|PDB:2FPQ}.
HELIX 313 318 {ECO:0000244|PDB:2FPQ}.
HELIX 319 329 {ECO:0000244|PDB:2FPQ}.
HELIX 344 355 {ECO:0000244|PDB:2FPQ}.
HELIX 360 366 {ECO:0000244|PDB:2FPQ}.
STRAND 380 384 {ECO:0000244|PDB:5BQM}.
TURN 390 392 {ECO:0000244|PDB:2FPQ}.
TURN 395 397 {ECO:0000244|PDB:2FPQ}.
HELIX 403 405 {ECO:0000244|PDB:2FPQ}.
STRAND 408 410 {ECO:0000244|PDB:5BQM}.
HELIX 411 413 {ECO:0000244|PDB:2FPQ}.
TURN 415 417 {ECO:0000244|PDB:2FPQ}.
STRAND 421 423 {ECO:0000244|PDB:2FPQ}.
TURN 426 428 {ECO:0000244|PDB:5BQN}.
STRAND 433 437 {ECO:0000244|PDB:5BQM}.
STRAND 451 454 {ECO:0000244|PDB:5BQN}.
TURN 464 466 {ECO:0000244|PDB:5BQM}.
HELIX 470 472 {ECO:0000244|PDB:5BQM}.
STRAND 493 500 {ECO:0000244|PDB:5BQN}.
STRAND 515 518 {ECO:0000244|PDB:5BQN}.
STRAND 525 527 {ECO:0000244|PDB:5BQN}.
STRAND 533 536 {ECO:0000244|PDB:5BQM}.
STRAND 537 540 {ECO:0000244|PDB:5BQN}.
HELIX 548 558 {ECO:0000244|PDB:5BQN}.
HELIX 560 564 {ECO:0000244|PDB:5BQN}.
HELIX 569 576 {ECO:0000244|PDB:5BQN}.
HELIX 579 587 {ECO:0000244|PDB:5BQM}.
STRAND 590 592 {ECO:0000244|PDB:5BQN}.
TURN 596 598 {ECO:0000244|PDB:5BQN}.
STRAND 600 606 {ECO:0000244|PDB:5BQN}.
STRAND 609 611 {ECO:0000244|PDB:5BQN}.
STRAND 615 619 {ECO:0000244|PDB:5BQN}.
STRAND 622 625 {ECO:0000244|PDB:5BQN}.
HELIX 628 632 {ECO:0000244|PDB:5BQM}.
TURN 638 641 {ECO:0000244|PDB:5BQM}.
HELIX 643 647 {ECO:0000244|PDB:5BQN}.
STRAND 654 657 {ECO:0000244|PDB:5BQN}.
TURN 680 682 {ECO:0000244|PDB:5BQN}.
HELIX 688 707 {ECO:0000244|PDB:5BQN}.
HELIX 721 724 {ECO:0000244|PDB:5BQN}.
HELIX 738 745 {ECO:0000244|PDB:5BQN}.
HELIX 749 751 {ECO:0000244|PDB:5BQN}.
HELIX 754 775 {ECO:0000244|PDB:5BQN}.
HELIX 792 802 {ECO:0000244|PDB:5BQN}.
HELIX 812 817 {ECO:0000244|PDB:5BQN}.
HELIX 828 834 {ECO:0000244|PDB:5BQN}.
HELIX 864 867 {ECO:0000244|PDB:3OGG}.
STRAND 868 875 {ECO:0000244|PDB:3OGG}.
STRAND 878 881 {ECO:0000244|PDB:3OGG}.
STRAND 883 885 {ECO:0000244|PDB:3OGG}.
STRAND 888 891 {ECO:0000244|PDB:3OGG}.
STRAND 896 901 {ECO:0000244|PDB:3OGG}.
STRAND 904 907 {ECO:0000244|PDB:3OGG}.
STRAND 909 911 {ECO:0000244|PDB:3OBT}.
STRAND 914 917 {ECO:0000244|PDB:3OGG}.
HELIX 919 921 {ECO:0000244|PDB:5BQN}.
STRAND 931 939 {ECO:0000244|PDB:3OGG}.
HELIX 941 944 {ECO:0000244|PDB:3OGG}.
STRAND 948 954 {ECO:0000244|PDB:3OGG}.
STRAND 957 959 {ECO:0000244|PDB:3OGG}.
STRAND 961 967 {ECO:0000244|PDB:3OGG}.
STRAND 970 976 {ECO:0000244|PDB:3OGG}.
STRAND 982 988 {ECO:0000244|PDB:3OGG}.
TURN 991 993 {ECO:0000244|PDB:3OGG}.
STRAND 1003 1009 {ECO:0000244|PDB:3OGG}.
STRAND 1013 1019 {ECO:0000244|PDB:3OGG}.
STRAND 1022 1028 {ECO:0000244|PDB:3OGG}.
HELIX 1030 1034 {ECO:0000244|PDB:5BQN}.
HELIX 1036 1038 {ECO:0000244|PDB:5BQN}.
STRAND 1040 1044 {ECO:0000244|PDB:3OGG}.
HELIX 1046 1049 {ECO:0000244|PDB:5BQN}.
HELIX 1051 1054 {ECO:0000244|PDB:5BQN}.
STRAND 1055 1065 {ECO:0000244|PDB:3OGG}.
HELIX 1069 1079 {ECO:0000244|PDB:3OGG}.
TURN 1080 1083 {ECO:0000244|PDB:3OGG}.
STRAND 1090 1092 {ECO:0000244|PDB:3OGG}.
STRAND 1098 1103 {ECO:0000244|PDB:3OGG}.
STRAND 1109 1114 {ECO:0000244|PDB:3OGG}.
STRAND 1117 1122 {ECO:0000244|PDB:3OGG}.
STRAND 1135 1139 {ECO:0000244|PDB:3OGG}.
STRAND 1150 1152 {ECO:0000244|PDB:3RMX}.
STRAND 1154 1161 {ECO:0000244|PDB:3OGG}.
STRAND 1164 1170 {ECO:0000244|PDB:3OGG}.
STRAND 1188 1196 {ECO:0000244|PDB:3OGG}.
HELIX 1201 1203 {ECO:0000244|PDB:3OGG}.
STRAND 1204 1209 {ECO:0000244|PDB:3OGG}.
STRAND 1218 1222 {ECO:0000244|PDB:3OGG}.
STRAND 1224 1226 {ECO:0000244|PDB:3OGG}.
STRAND 1228 1235 {ECO:0000244|PDB:3OGG}.
TURN 1239 1242 {ECO:0000244|PDB:3RMY}.
STRAND 1245 1253 {ECO:0000244|PDB:3OGG}.
HELIX 1255 1257 {ECO:0000244|PDB:3OGG}.
HELIX 1261 1263 {ECO:0000244|PDB:3OGG}.
STRAND 1265 1268 {ECO:0000244|PDB:3OGG}.
SEQUENCE 1276 AA; 146872 MW; C1EC50F46C8233E2 CRC64;
MTWPVKDFNY SDPVNDNDIL YLRIPQNKLI TTPVKAFMIT QNIWVIPERF SSDTNPSLSK
PPRPTSKYQS YYDPSYLSTD EQKDTFLKGI IKLFKRINER DIGKKLINYL VVGSPFMGDS
STPEDTFDFT RHTTNIAVEK FENGSWKVTN IITPSVLIFG PLPNILDYTA SLTLQGQQSN
PSFEGFGTLS ILKVAPEFLL TFSDVTSNQS SAVLGKSIFC MDPVIALMHE LTHSLHQLYG
INIPSDKRIR PQVSEGFFSQ DGPNVQFEEL YTFGGLDVEI IPQIERSQLR EKALGHYKDI
AKRLNNINKT IPSSWISNID KYKKIFSEKY NFDKDNTGNF VVNIDKFNSL YSDLTNVMSE
VVYSSQYNVK NRTHYFSRHY LPVFANILDD NIYTIRDGFN LTNKGFNIEN SGQNIERNPA
LQKLSSESVV DLFTKVCLRL TKNSRDDSTC IKVKNNRLPY VADKDSISQE IFENKIITDE
TNVQNYSDKF SLDESILDGQ VPINPEIVDP LLPNVNMEPL NLPGEEIVFY DDITKYVDYL
NSYYYLESQK LSNNVENITL TTSVEEALGY SNKIYTFLPS LAEKVNKGVQ AGLFLNWANE
VVEDFTTNIM KKDTLDKISD VSVIIPYIGP ALNIGNSALR GNFNQAFATA GVAFLLEGFP
EFTIPALGVF TFYSSIQERE KIIKTIENCL EQRVKRWKDS YQWMVSNWLS RITTQFNHIN
YQMYDSLSYQ ADAIKAKIDL EYKKYSGSDK ENIKSQVENL KNSLDVKISE AMNNINKFIR
ECSVTYLFKN MLPKVIDELN KFDLRTKTEL INLIDSHNII LVGEVDRLKA KVNESFENTM
PFNIFSYTNN SLLKDIINEY FNSINDSKIL SLQNKKNALV DTSGYNAEVR VGDNVQLNTI
YTNDFKLSSS GDKIIVNLNN NILYSAIYEN SSVSFWIKIS KDLTNSHNEY TIINSIEQNS
GWKLCIRNGN IEWILQDVNR KYKSLIFDYS ESLSHTGYTN KWFFVTITNN IMGYMKLYIN
GELKQSQKIE DLDEVKLDKT IVFGIDENID ENQMLWIRDF NIFSKELSNE DINIVYEGQI
LRNVIKDYWG NPLKFDTEYY IINDNYIDRY IAPESNVLVL VQYPDRSKLY TGNPITIKSV
SDKNPYSRIL NGDNIILHML YNSRKYMIIR DTDTIYATQG GECSQNCVYA LKLQSNLGNY
GIGIFSIKNI VSKNKYCSQI FSSFRENTML LADIYKPWRF SFKNAYTPVA VTNYETKLLS
TSSFWKFISR DPGWVE


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