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P19321 (BXD_CLOBO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Botulinum neurotoxin type D

Short name=BoNT/D
EC=3.4.24.69
Alternative name(s):
Bontoxilysin-D
Gene names
Name:botD
OrganismClostridium botulinum
Taxonomic identifier1491 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length1276 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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

Binds 1 zinc ion per subunit By similarity.

Subunit structure

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.

Subcellular location

Botulinum neurotoxin D light chain: Secreted. Host cytoplasmhost cytosol.

Botulinum neurotoxin D heavy chain: Secreted. Host cell junctionhost synapsehost presynaptic cell membrane Potential.

Miscellaneous

There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.

Botulinum type D neurotoxin is synthesized by D strains of C.botulinum which carry the appropriate bacteriophage.

Sequence similarities

Belongs to the peptidase M27 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 442442Botulinum neurotoxin D light chain
PRO_0000029219
Chain443 – 1276834Botulinum neurotoxin D heavy chain
PRO_0000029220

Sites

Active site2301 By similarity
Metal binding2291Zinc; catalytic
Metal binding2331Zinc; catalytic
Metal binding2691Zinc; catalytic

Amino acid modifications

Disulfide bond437 ↔ 450Interchain (between light and heavy chains) Probable

Natural variations

Natural variant15 – 162ND → PV in strain: D-SA.
Natural variant17 – 182ND → LQ in strain: D-1873.
Natural variant4521K → Q in strain: D-SA.
Natural variant4571R → F in strain: D-1873.
Natural variant4571R → T in strain: D-SA.
Natural variant4621A → D in strain: D-1873.
Natural variant4891K → N in strain: CB16.
Natural variant6441N → K in strain: CB16.
Natural variant11221Q → R in strain: CB16.

Secondary structure

............................................................................................................................................... 1276
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19321 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: C1EC50F46C8233E2

FASTA1,276146,872
        10         20         30         40         50         60 
MTWPVKDFNY SDPVNDNDIL YLRIPQNKLI TTPVKAFMIT QNIWVIPERF SSDTNPSLSK 

        70         80         90        100        110        120 
PPRPTSKYQS YYDPSYLSTD EQKDTFLKGI IKLFKRINER DIGKKLINYL VVGSPFMGDS 

       130        140        150        160        170        180 
STPEDTFDFT RHTTNIAVEK FENGSWKVTN IITPSVLIFG PLPNILDYTA SLTLQGQQSN 

       190        200        210        220        230        240 
PSFEGFGTLS ILKVAPEFLL TFSDVTSNQS SAVLGKSIFC MDPVIALMHE LTHSLHQLYG 

       250        260        270        280        290        300 
INIPSDKRIR PQVSEGFFSQ DGPNVQFEEL YTFGGLDVEI IPQIERSQLR EKALGHYKDI 

       310        320        330        340        350        360 
AKRLNNINKT IPSSWISNID KYKKIFSEKY NFDKDNTGNF VVNIDKFNSL YSDLTNVMSE 

       370        380        390        400        410        420 
VVYSSQYNVK NRTHYFSRHY LPVFANILDD NIYTIRDGFN LTNKGFNIEN SGQNIERNPA 

       430        440        450        460        470        480 
LQKLSSESVV DLFTKVCLRL TKNSRDDSTC IKVKNNRLPY VADKDSISQE IFENKIITDE 

       490        500        510        520        530        540 
TNVQNYSDKF SLDESILDGQ VPINPEIVDP LLPNVNMEPL NLPGEEIVFY DDITKYVDYL 

       550        560        570        580        590        600 
NSYYYLESQK LSNNVENITL TTSVEEALGY SNKIYTFLPS LAEKVNKGVQ AGLFLNWANE 

       610        620        630        640        650        660 
VVEDFTTNIM KKDTLDKISD VSVIIPYIGP ALNIGNSALR GNFNQAFATA GVAFLLEGFP 

       670        680        690        700        710        720 
EFTIPALGVF TFYSSIQERE KIIKTIENCL EQRVKRWKDS YQWMVSNWLS RITTQFNHIN 

       730        740        750        760        770        780 
YQMYDSLSYQ ADAIKAKIDL EYKKYSGSDK ENIKSQVENL KNSLDVKISE AMNNINKFIR 

       790        800        810        820        830        840 
ECSVTYLFKN MLPKVIDELN KFDLRTKTEL INLIDSHNII LVGEVDRLKA KVNESFENTM 

       850        860        870        880        890        900 
PFNIFSYTNN SLLKDIINEY FNSINDSKIL SLQNKKNALV DTSGYNAEVR VGDNVQLNTI 

       910        920        930        940        950        960 
YTNDFKLSSS GDKIIVNLNN NILYSAIYEN SSVSFWIKIS KDLTNSHNEY TIINSIEQNS 

       970        980        990       1000       1010       1020 
GWKLCIRNGN IEWILQDVNR KYKSLIFDYS ESLSHTGYTN KWFFVTITNN IMGYMKLYIN 

      1030       1040       1050       1060       1070       1080 
GELKQSQKIE DLDEVKLDKT IVFGIDENID ENQMLWIRDF NIFSKELSNE DINIVYEGQI 

      1090       1100       1110       1120       1130       1140 
LRNVIKDYWG NPLKFDTEYY IINDNYIDRY IAPESNVLVL VQYPDRSKLY TGNPITIKSV 

      1150       1160       1170       1180       1190       1200 
SDKNPYSRIL NGDNIILHML YNSRKYMIIR DTDTIYATQG GECSQNCVYA LKLQSNLGNY 

      1210       1220       1230       1240       1250       1260 
GIGIFSIKNI VSKNKYCSQI FSSFRENTML LADIYKPWRF SFKNAYTPVA VTNYETKLLS 

      1270 
TSSFWKFISR DPGWVE 

« Hide

References

[1]"Nucleotide sequence of the gene encoding Clostridium botulinum neurotoxin type D."
Binz T., Kurazono H., Popoff M.R., Eklund M.W., Sakaguchi G., Kozaki S., Krieglstein K., Henschen A., Gill D.M., Niemann H.
Nucleic Acids Res. 18:5556-5556(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Type D / BVD/-3.
[2]"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."
Sunagawa H., Ohyama T., Watanabe T., Inoue K.
J. Vet. Med. Sci. 54:905-913(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Type D / CB-16.
[3]"Molecular diversity of neurotoxins from Clostridium botulinum type D strains."
Moriishi K., Syuto B., Kubo S., Oguma K.
Infect. Immun. 57:2886-2891(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Strain: Type D / D-1873 and Type D / South African.
[4]"Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin."
Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F., Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H.
J. Biol. Chem. 269:12764-12772(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF SUBSTRATE.
[5]"Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity."
Arndt J.W., Chai Q., Christian T., Stevens R.C.
Biochemistry 45:3255-3262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-436 IN COMPLEX WITH ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54254 Genomic DNA. Translation: CAA38175.1.
S49407 Genomic DNA. Translation: AAB24244.1.
PIRS11455.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FPQX-ray1.65A1-436[»]
3N7JX-ray2.00A862-1276[»]
3OBRX-ray1.72A863-1276[»]
3OBTX-ray2.00A863-1276[»]
3OGGX-ray1.65A863-1276[»]
3RMXX-ray2.75A/B/C/D862-1276[»]
3RMYX-ray2.30A/B/C/D862-1276[»]
ProteinModelPortalP19321.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM27.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_13685. Neuronal System.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR011065. Kunitz_inhibitor_ST1-like.
IPR000395. Neurotox_Zn_protease.
IPR013104. Toxin_rcpt-bd_C.
IPR012928. Toxin_rcpt-bd_N.
IPR012500. Toxin_trans.
[Graphical view]
PfamPF01742. Peptidase_M27. 1 hit.
PF07951. Toxin_R_bind_C. 1 hit.
PF07953. Toxin_R_bind_N. 1 hit.
PF07952. Toxin_trans. 1 hit.
[Graphical view]
PRINTSPR00760. BONTOXILYSIN.
SUPFAMSSF49899. SSF49899. 1 hit.
SSF50386. SSF50386. 2 hits.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19321.

Entry information

Entry nameBXD_CLOBO
AccessionPrimary (citable) accession number: P19321
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references