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Q5EK40

- CHXA_VIBCL

UniProt

Q5EK40 - CHXA_VIBCL

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Protein
Cholix toxin
Gene
chxA, toxA
Organism
Vibrio cholerae
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

An NAD-dependent ADP-ribosyltransferase (ADPRT), it catalyzes the transfer of the ADP-ribosyl moiety of oxidized NAD onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. It probably uses the eukaryotic prolow-density lipoprotein receptor-related protein 1 (LRP1) to enter mouse cells, although there seems to be at least one other receptor as well. Is active against mouse fibroblasts, Chinese hamster ovary eEF-2, brine shrimp (Artemia spp. nauplii) and upon expression in S.cerevisiae.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

Kineticsi

For ADP-ribosyltransferase activity of a catalytic fragment of residues 459-666.

  1. KM=45 µM for NAD1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei613 – 6131 Inferred

GO - Molecular functioni

  1. NAD+-diphthamide ADP-ribosyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Toxin, Transferase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Cholix toxin (EC:2.4.2.36)
Alternative name(s):
Exotoxin A
NAD(+)--diphthamide ADP-ribosyltransferase
Gene namesi
Name:chxA
Synonyms:toxA
OrganismiVibrio cholerae
Taxonomic identifieri666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi606 – 6061E → A: Loss of ADPRT activity, loss of toxicity against yeast. 1 Publication
Mutagenesisi613 – 6131E → A: Loss of ADPRT activity, loss of toxicity against mouse cells, brine shrimp and yeast. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232 Reviewed prediction
Add
BLAST
Chaini33 – 666634Cholix toxin
PRO_0000409819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 47
Disulfide bondi240 ↔ 257
Disulfide bondi310 ↔ 332
Disulfide bondi426 ↔ 433

Post-translational modificationi

Probably requires further proteolytic processing to generate a fragment with toxic activity.

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 424
Beta strandi47 – 493
Beta strandi57 – 626
Beta strandi71 – 8111
Beta strandi94 – 996
Turni100 – 1023
Beta strandi103 – 1086
Beta strandi113 – 1153
Beta strandi120 – 1267
Beta strandi131 – 1377
Beta strandi139 – 15214
Beta strandi157 – 16610
Beta strandi170 – 1723
Beta strandi177 – 1826
Helixi185 – 1906
Turni191 – 1933
Beta strandi194 – 20310
Beta strandi208 – 21912
Helixi226 – 2305
Helixi231 – 2344
Helixi236 – 2416
Helixi245 – 2484
Beta strandi269 – 2735
Beta strandi289 – 2935
Helixi300 – 31011
Helixi314 – 3174
Helixi328 – 34619
Helixi350 – 3545
Helixi355 – 3584
Helixi361 – 3633
Helixi366 – 38116
Helixi385 – 40319
Helixi409 – 41810
Beta strandi420 – 4256
Beta strandi441 – 4455
Helixi450 – 4534
Beta strandi460 – 4623
Beta strandi465 – 4684
Helixi471 – 48313
Beta strandi486 – 4949
Helixi496 – 5049
Helixi516 – 5205
Beta strandi523 – 5297
Helixi530 – 5345
Helixi545 – 5473
Helixi551 – 5555
Beta strandi559 – 5668
Helixi567 – 5726
Beta strandi573 – 5753
Helixi580 – 5823
Helixi584 – 5918
Beta strandi601 – 6077
Beta strandi612 – 6165
Helixi618 – 6214
Beta strandi625 – 6328
Helixi643 – 6497
Helixi650 – 6523
Helixi662 – 6643

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q5TX-ray2.10A33-666[»]
2Q6MX-ray1.25A459-666[»]
3ESSX-ray1.19A459-665[»]
3KI0X-ray1.29A459-665[»]
3KI1X-ray1.43A459-665[»]
3KI2X-ray1.28A459-665[»]
3KI3X-ray1.27A459-665[»]
3KI4X-ray1.65A459-665[»]
3KI5X-ray1.55A459-665[»]
3KI6X-ray1.54A459-665[»]
3KI7X-ray1.32A459-665[»]
3NY6X-ray1.68A459-665[»]
3Q9OX-ray1.79A33-666[»]
ProteinModelPortaliQ5EK40.
SMRiQ5EK40. Positions 37-662.

Miscellaneous databases

EvolutionaryTraceiQ5EK40.

Family & Domainsi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1350.10. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR015185. Exotox-A_bind.
IPR015099. Exotox-A_cataly_dom.
IPR015186. Exotox-A_middle_dom.
[Graphical view]
PfamiPF09101. Exotox-A_bind. 1 hit.
PF09009. Exotox-A_cataly. 1 hit.
PF09102. Exotox-A_target. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF56864. SSF56864. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5EK40-1 [UniParc]FASTAAdd to Basket

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MYLTFYLEKV MKKMLLIAGA TVISSMAHPT FAVEDELNIF DECRSPCSLT    50
PEPGKPIQSK LSIPSDVVLD EGVLYYSMTI NDEQNDIKDE DKGESIITIG 100
EFATVRATRH YVNQDAPFGV IHLDITTENG TKTYSYNRKE GEFAINWLVP 150
IGEDSPASIK ISVDELDQQR NIIEVPKLYS IDLDNQTLEQ WKTQGNVSFS 200
VTRPEHNIAI SWPSVSYKAA QKEGSRHKRW AHWHTGLALC WLVPMDAIYN 250
YITQQNCTLG DNWFGGSYET VAGTPKVITV KQGIEQKPVE QRIHFSKGNA 300
MSALAAHRVC GVPLETLARS RKPRDLTDDL SCAYQAQNIV SLFVATRILF 350
SHLDSVFTLN LDEQEPEVAE RLSDLRRINE NNPGMVTQVL TVARQIYNDY 400
VTHHPGLTPE QTSAGAQAAD ILSLFCPDAD KSCVASNNDQ ANINIESRSG 450
RSYLPENRAV ITPQGVTNWT YQELEATHQA LTREGYVFVG YHGTNHVAAQ 500
TIVNRIAPVP RGNNTENEEK WGGLYVATHA EVAHGYARIK EGTGEYGLPT 550
RAERDARGVM LRVYIPRASL ERFYRTNTPL ENAEEHITQV IGHSLPLRNE 600
AFTGPESAGG EDETVIGWDM AIHAVAIPST IPGNAYEELA IDEEAVAKEQ 650
SISTKPPYKE RKDELK 666
Length:666
Mass (Da):74,293
Last modified:March 15, 2005 - v1
Checksum:i3A76A86E0BC7FDD7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY876053 Genomic DNA. Translation: AAW80252.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY876053 Genomic DNA. Translation: AAW80252.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Q5T X-ray 2.10 A 33-666 [» ]
2Q6M X-ray 1.25 A 459-666 [» ]
3ESS X-ray 1.19 A 459-665 [» ]
3KI0 X-ray 1.29 A 459-665 [» ]
3KI1 X-ray 1.43 A 459-665 [» ]
3KI2 X-ray 1.28 A 459-665 [» ]
3KI3 X-ray 1.27 A 459-665 [» ]
3KI4 X-ray 1.65 A 459-665 [» ]
3KI5 X-ray 1.55 A 459-665 [» ]
3KI6 X-ray 1.54 A 459-665 [» ]
3KI7 X-ray 1.32 A 459-665 [» ]
3NY6 X-ray 1.68 A 459-665 [» ]
3Q9O X-ray 1.79 A 33-666 [» ]
ProteinModelPortali Q5EK40.
SMRi Q5EK40. Positions 37-662.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q5EK40.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
3.90.1350.10. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR015185. Exotox-A_bind.
IPR015099. Exotox-A_cataly_dom.
IPR015186. Exotox-A_middle_dom.
[Graphical view ]
Pfami PF09101. Exotox-A_bind. 1 hit.
PF09009. Exotox-A_cataly. 1 hit.
PF09102. Exotox-A_target. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF56864. SSF56864. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "A glimpse into the expanded genome content of Vibrio cholerae through identification of genes present in environmental strains."
    Purdy A., Rohwer F., Edwards R., Azam F., Bartlett D.H.
    J. Bacteriol. 187:2992-3001(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: TP.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 459-666 IN COMPLEX WITH INHIBITOR AND (2.1 ANGSTROMS) OF 33-666, FUNCTION AS A TOXIN, FUNCTION AS A GLYCOHYDROLASE, FUNCTION AS AN ADP-RIBOSYLTRANSFERASE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-613.
    Strain: TP.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) OF 459-665 IN COMPLEX WITH INHIBITOR, FUNCTION AS A TOXIN, ENZYME REGULATION, MUTAGENESIS OF GLU-606.
    Strain: TP.
  4. "Newly discovered and characterized antivirulence compounds inhibit bacterial mono-ADP-ribosyltransferase toxins."
    Turgeon Z., Jorgensen R., Visschedyk D., Edwards P.R., Legree S., McGregor C., Fieldhouse R.J., Mangroo D., Schapira M., Merrill A.R.
    Antimicrob. Agents Chemother. 55:983-991(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF 459-665 IN COMPLEX WITH INHIBITORS.
    Strain: TP.

Entry informationi

Entry nameiCHXA_VIBCL
AccessioniPrimary (citable) accession number: Q5EK40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Exotoxins are often highly strain specific; not encoded in strain ATCC 39315 / El Tor Inabe N16961.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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