Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Botulinum neurotoxin type D

Gene

botD

Organism
Clostridium botulinum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi229Zinc; catalytic1
Active sitei230PROSITE-ProRule annotation1
Metal bindingi233Zinc; catalytic1
Metal bindingi269Zinc; catalytic1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250955. Toxicity of botulinum toxin type D (BoNT/D).

Names & Taxonomyi

Protein namesi
Recommended name:
Botulinum neurotoxin type D (EC:3.4.24.69)
Short name:
BoNT/D
Alternative name(s):
Bontoxilysin-D
Cleaved into the following 2 chains:
Gene namesi
Name:botD
OrganismiClostridium botulinum
Taxonomic identifieri1491 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell junction, Host cell membrane, Host cytoplasm, Host membrane, Host synapse, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000292191 – 442Botulinum neurotoxin D light chainAdd BLAST442
ChainiPRO_0000029220443 – 1276Botulinum neurotoxin D heavy chainAdd BLAST834

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi437 ↔ 450Interchain (between light and heavy chains)Curated

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

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.1 Publication

Structurei

Secondary structure

11276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 23Combined sources8
Beta strandi34 – 40Combined sources7
Beta strandi43 – 46Combined sources4
Beta strandi53 – 55Combined sources3
Turni67 – 69Combined sources3
Turni74 – 77Combined sources4
Helixi80 – 97Combined sources18
Helixi101 – 112Combined sources12
Beta strandi120 – 122Combined sources3
Beta strandi126 – 128Combined sources3
Turni132 – 134Combined sources3
Beta strandi136 – 142Combined sources7
Beta strandi145 – 152Combined sources8
Beta strandi155 – 159Combined sources5
Helixi170 – 172Combined sources3
Helixi176 – 178Combined sources3
Helixi181 – 183Combined sources3
Beta strandi184 – 186Combined sources3
Beta strandi190 – 193Combined sources4
Beta strandi201 – 203Combined sources3
Turni212 – 214Combined sources3
Beta strandi218 – 220Combined sources3
Helixi223 – 238Combined sources16
Beta strandi247 – 249Combined sources3
Helixi267 – 273Combined sources7
Helixi275 – 280Combined sources6
Helixi283 – 306Combined sources24
Beta strandi309 – 312Combined sources4
Helixi313 – 318Combined sources6
Helixi319 – 329Combined sources11
Helixi344 – 355Combined sources12
Helixi360 – 366Combined sources7
Beta strandi380 – 384Combined sources5
Turni390 – 392Combined sources3
Turni395 – 397Combined sources3
Helixi403 – 405Combined sources3
Beta strandi408 – 410Combined sources3
Helixi411 – 413Combined sources3
Turni415 – 417Combined sources3
Beta strandi421 – 423Combined sources3
Turni426 – 428Combined sources3
Beta strandi433 – 437Combined sources5
Beta strandi451 – 454Combined sources4
Helixi455 – 457Combined sources3
Helixi464 – 466Combined sources3
Helixi470 – 472Combined sources3
Beta strandi533 – 539Combined sources7
Helixi542 – 548Combined sources7
Beta strandi559 – 562Combined sources4
Helixi564 – 569Combined sources6
Beta strandi573 – 575Combined sources3
Helixi579 – 586Combined sources8
Helixi594 – 609Combined sources16
Beta strandi620 – 624Combined sources5
Helixi628 – 632Combined sources5
Turni638 – 641Combined sources4
Helixi643 – 650Combined sources8
Helixi652 – 655Combined sources4
Helixi680 – 682Combined sources3
Helixi684 – 711Combined sources28
Helixi713 – 744Combined sources32
Turni748 – 753Combined sources6
Helixi754 – 762Combined sources9
Helixi764 – 789Combined sources26
Helixi792 – 816Combined sources25
Turni817 – 821Combined sources5
Helixi828 – 832Combined sources5
Turni833 – 836Combined sources4
Beta strandi844 – 846Combined sources3
Helixi847 – 849Combined sources3
Helixi850 – 860Combined sources11
Helixi864 – 867Combined sources4
Beta strandi868 – 875Combined sources8
Beta strandi878 – 881Combined sources4
Beta strandi883 – 885Combined sources3
Beta strandi888 – 891Combined sources4
Beta strandi896 – 901Combined sources6
Beta strandi904 – 907Combined sources4
Beta strandi909 – 911Combined sources3
Beta strandi914 – 917Combined sources4
Beta strandi931 – 939Combined sources9
Helixi941 – 944Combined sources4
Beta strandi948 – 954Combined sources7
Beta strandi957 – 959Combined sources3
Beta strandi961 – 967Combined sources7
Beta strandi970 – 976Combined sources7
Beta strandi982 – 988Combined sources7
Turni991 – 993Combined sources3
Beta strandi1003 – 1009Combined sources7
Beta strandi1013 – 1019Combined sources7
Beta strandi1022 – 1028Combined sources7
Beta strandi1040 – 1044Combined sources5
Beta strandi1055 – 1065Combined sources11
Helixi1069 – 1079Combined sources11
Turni1080 – 1083Combined sources4
Beta strandi1090 – 1092Combined sources3
Beta strandi1098 – 1103Combined sources6
Beta strandi1109 – 1114Combined sources6
Beta strandi1117 – 1122Combined sources6
Beta strandi1135 – 1139Combined sources5
Beta strandi1150 – 1152Combined sources3
Beta strandi1154 – 1161Combined sources8
Beta strandi1164 – 1170Combined sources7
Beta strandi1188 – 1196Combined sources9
Helixi1201 – 1203Combined sources3
Beta strandi1204 – 1209Combined sources6
Beta strandi1218 – 1222Combined sources5
Beta strandi1224 – 1226Combined sources3
Beta strandi1228 – 1235Combined sources8
Turni1239 – 1242Combined sources4
Beta strandi1245 – 1253Combined sources9
Helixi1255 – 1257Combined sources3
Helixi1261 – 1263Combined sources3
Beta strandi1265 – 1268Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5BQMX-ray3.10A/C1-437[»]
B/D450-861[»]
5BQNX-ray2.30A1-437[»]
A450-862[»]
ProteinModelPortaliP19321.
SMRiP19321.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19321.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

Keywords - Domaini

Transmembrane

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
IPR013104. Toxin_rcpt-bd_C.
IPR012928. Toxin_rcpt-bd_N.
IPR012500. Toxin_trans.
[Graphical view]
PfamiPF01742. 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]
PRINTSiPR00760. BONTOXILYSIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50386. SSF50386. 2 hits.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P19321-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTWPVKDFNY SDPVNDNDIL YLRIPQNKLI TTPVKAFMIT QNIWVIPERF
60 70 80 90 100
SSDTNPSLSK PPRPTSKYQS YYDPSYLSTD EQKDTFLKGI IKLFKRINER
110 120 130 140 150
DIGKKLINYL VVGSPFMGDS STPEDTFDFT RHTTNIAVEK FENGSWKVTN
160 170 180 190 200
IITPSVLIFG PLPNILDYTA SLTLQGQQSN PSFEGFGTLS ILKVAPEFLL
210 220 230 240 250
TFSDVTSNQS SAVLGKSIFC MDPVIALMHE LTHSLHQLYG INIPSDKRIR
260 270 280 290 300
PQVSEGFFSQ DGPNVQFEEL YTFGGLDVEI IPQIERSQLR EKALGHYKDI
310 320 330 340 350
AKRLNNINKT IPSSWISNID KYKKIFSEKY NFDKDNTGNF VVNIDKFNSL
360 370 380 390 400
YSDLTNVMSE VVYSSQYNVK NRTHYFSRHY LPVFANILDD NIYTIRDGFN
410 420 430 440 450
LTNKGFNIEN SGQNIERNPA LQKLSSESVV DLFTKVCLRL TKNSRDDSTC
460 470 480 490 500
IKVKNNRLPY VADKDSISQE IFENKIITDE TNVQNYSDKF SLDESILDGQ
510 520 530 540 550
VPINPEIVDP LLPNVNMEPL NLPGEEIVFY DDITKYVDYL NSYYYLESQK
560 570 580 590 600
LSNNVENITL TTSVEEALGY SNKIYTFLPS LAEKVNKGVQ AGLFLNWANE
610 620 630 640 650
VVEDFTTNIM KKDTLDKISD VSVIIPYIGP ALNIGNSALR GNFNQAFATA
660 670 680 690 700
GVAFLLEGFP EFTIPALGVF TFYSSIQERE KIIKTIENCL EQRVKRWKDS
710 720 730 740 750
YQWMVSNWLS RITTQFNHIN YQMYDSLSYQ ADAIKAKIDL EYKKYSGSDK
760 770 780 790 800
ENIKSQVENL KNSLDVKISE AMNNINKFIR ECSVTYLFKN MLPKVIDELN
810 820 830 840 850
KFDLRTKTEL INLIDSHNII LVGEVDRLKA KVNESFENTM PFNIFSYTNN
860 870 880 890 900
SLLKDIINEY FNSINDSKIL SLQNKKNALV DTSGYNAEVR VGDNVQLNTI
910 920 930 940 950
YTNDFKLSSS GDKIIVNLNN NILYSAIYEN SSVSFWIKIS KDLTNSHNEY
960 970 980 990 1000
TIINSIEQNS GWKLCIRNGN IEWILQDVNR KYKSLIFDYS ESLSHTGYTN
1010 1020 1030 1040 1050
KWFFVTITNN IMGYMKLYIN GELKQSQKIE DLDEVKLDKT IVFGIDENID
1060 1070 1080 1090 1100
ENQMLWIRDF NIFSKELSNE DINIVYEGQI LRNVIKDYWG NPLKFDTEYY
1110 1120 1130 1140 1150
IINDNYIDRY IAPESNVLVL VQYPDRSKLY TGNPITIKSV SDKNPYSRIL
1160 1170 1180 1190 1200
NGDNIILHML YNSRKYMIIR DTDTIYATQG GECSQNCVYA LKLQSNLGNY
1210 1220 1230 1240 1250
GIGIFSIKNI VSKNKYCSQI FSSFRENTML LADIYKPWRF SFKNAYTPVA
1260 1270
VTNYETKLLS TSSFWKFISR DPGWVE
Length:1,276
Mass (Da):146,872
Last modified:November 1, 1990 - v1
Checksum:iC1EC50F46C8233E2
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti15 – 16ND → PV in strain: D-SA. 2
Natural varianti17 – 18ND → LQ in strain: D-1873. 2
Natural varianti452K → Q in strain: D-SA. 1
Natural varianti457R → F in strain: D-1873. 1
Natural varianti457R → T in strain: D-SA. 1
Natural varianti462A → D in strain: D-1873. 1
Natural varianti489K → N in strain: CB16. 1
Natural varianti644N → K in strain: CB16. 1
Natural varianti1122Q → R in strain: CB16. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54254 Genomic DNA. Translation: CAA38175.1.
S49407 Genomic DNA. Translation: AAB24244.1.
PIRiS11455.

Cross-referencesi

Web resourcesi

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54254 Genomic DNA. Translation: CAA38175.1.
S49407 Genomic DNA. Translation: AAB24244.1.
PIRiS11455.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5BQMX-ray3.10A/C1-437[»]
B/D450-861[»]
5BQNX-ray2.30A1-437[»]
A450-862[»]
ProteinModelPortaliP19321.
SMRiP19321.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250955. Toxicity of botulinum toxin type D (BoNT/D).

Miscellaneous databases

EvolutionaryTraceiP19321.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
IPR013104. Toxin_rcpt-bd_C.
IPR012928. Toxin_rcpt-bd_N.
IPR012500. Toxin_trans.
[Graphical view]
PfamiPF01742. 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]
PRINTSiPR00760. BONTOXILYSIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50386. SSF50386. 2 hits.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBXD_CLOBO
AccessioniPrimary (citable) accession number: P19321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.