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Protein

Cholix toxin

Gene

chxA

Organism
Vibrio cholerae
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
    Active sitei613Curated1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Toxin, Transferase

    Keywords - Ligandi

    NAD

    Protein family/group databases

    TCDBi1.C.73.1.2. the pseudomonas exotoxin a (p-exoa) family.

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi606E → A: Loss of ADPRT activity, loss of toxicity against yeast. 1 Publication1
    Mutagenesisi613E → A: Loss of ADPRT activity, loss of toxicity against mouse cells, brine shrimp and yeast. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 32Sequence analysisAdd BLAST32
    ChainiPRO_000040981933 – 666Cholix toxinAdd BLAST634

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    1666
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi39 – 42Combined sources4
    Beta strandi47 – 49Combined sources3
    Beta strandi57 – 62Combined sources6
    Beta strandi71 – 81Combined sources11
    Beta strandi94 – 99Combined sources6
    Turni100 – 102Combined sources3
    Beta strandi103 – 108Combined sources6
    Beta strandi113 – 115Combined sources3
    Beta strandi120 – 126Combined sources7
    Beta strandi131 – 137Combined sources7
    Beta strandi139 – 152Combined sources14
    Beta strandi157 – 166Combined sources10
    Beta strandi170 – 172Combined sources3
    Beta strandi177 – 182Combined sources6
    Helixi185 – 190Combined sources6
    Turni191 – 193Combined sources3
    Beta strandi194 – 203Combined sources10
    Beta strandi208 – 219Combined sources12
    Helixi226 – 230Combined sources5
    Helixi231 – 234Combined sources4
    Helixi236 – 241Combined sources6
    Helixi245 – 248Combined sources4
    Beta strandi269 – 273Combined sources5
    Beta strandi289 – 293Combined sources5
    Helixi300 – 310Combined sources11
    Helixi314 – 317Combined sources4
    Helixi328 – 346Combined sources19
    Helixi350 – 354Combined sources5
    Helixi355 – 358Combined sources4
    Helixi361 – 363Combined sources3
    Helixi366 – 381Combined sources16
    Helixi385 – 403Combined sources19
    Helixi409 – 418Combined sources10
    Beta strandi420 – 425Combined sources6
    Beta strandi441 – 445Combined sources5
    Helixi450 – 453Combined sources4
    Beta strandi460 – 462Combined sources3
    Beta strandi465 – 468Combined sources4
    Helixi471 – 483Combined sources13
    Beta strandi486 – 494Combined sources9
    Helixi496 – 504Combined sources9
    Helixi516 – 520Combined sources5
    Beta strandi523 – 529Combined sources7
    Helixi530 – 534Combined sources5
    Helixi545 – 547Combined sources3
    Helixi551 – 555Combined sources5
    Beta strandi559 – 566Combined sources8
    Helixi567 – 572Combined sources6
    Beta strandi573 – 575Combined sources3
    Helixi580 – 582Combined sources3
    Helixi584 – 591Combined sources8
    Beta strandi601 – 607Combined sources7
    Beta strandi612 – 616Combined sources5
    Helixi618 – 621Combined sources4
    Beta strandi625 – 632Combined sources8
    Helixi643 – 649Combined sources7
    Helixi650 – 652Combined sources3
    Helixi662 – 664Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5EK40.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Family and domain databases

    CDDicd01436. Dipth_tox_like. 1 hit.
    Gene3Di2.60.120.200. 1 hit.
    3.90.1350.10. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    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

    « Hide

            10         20         30         40         50
    MYLTFYLEKV MKKMLLIAGA TVISSMAHPT FAVEDELNIF DECRSPCSLT
    60 70 80 90 100
    PEPGKPIQSK LSIPSDVVLD EGVLYYSMTI NDEQNDIKDE DKGESIITIG
    110 120 130 140 150
    EFATVRATRH YVNQDAPFGV IHLDITTENG TKTYSYNRKE GEFAINWLVP
    160 170 180 190 200
    IGEDSPASIK ISVDELDQQR NIIEVPKLYS IDLDNQTLEQ WKTQGNVSFS
    210 220 230 240 250
    VTRPEHNIAI SWPSVSYKAA QKEGSRHKRW AHWHTGLALC WLVPMDAIYN
    260 270 280 290 300
    YITQQNCTLG DNWFGGSYET VAGTPKVITV KQGIEQKPVE QRIHFSKGNA
    310 320 330 340 350
    MSALAAHRVC GVPLETLARS RKPRDLTDDL SCAYQAQNIV SLFVATRILF
    360 370 380 390 400
    SHLDSVFTLN LDEQEPEVAE RLSDLRRINE NNPGMVTQVL TVARQIYNDY
    410 420 430 440 450
    VTHHPGLTPE QTSAGAQAAD ILSLFCPDAD KSCVASNNDQ ANINIESRSG
    460 470 480 490 500
    RSYLPENRAV ITPQGVTNWT YQELEATHQA LTREGYVFVG YHGTNHVAAQ
    510 520 530 540 550
    TIVNRIAPVP RGNNTENEEK WGGLYVATHA EVAHGYARIK EGTGEYGLPT
    560 570 580 590 600
    RAERDARGVM LRVYIPRASL ERFYRTNTPL ENAEEHITQV IGHSLPLRNE
    610 620 630 640 650
    AFTGPESAGG EDETVIGWDM AIHAVAIPST IPGNAYEELA IDEEAVAKEQ
    660
    SISTKPPYKE RKDELK
    Length:666
    Mass (Da):74,293
    Last modified:March 15, 2005 - v1
    Checksum:i3A76A86E0BC7FDD7
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY876053 Genomic DNA. Translation: AAW80252.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY876053 Genomic DNA. Translation: AAW80252.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    TCDBi1.C.73.1.2. the pseudomonas exotoxin a (p-exoa) family.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5EK40.

    Family and domain databases

    CDDicd01436. Dipth_tox_like. 1 hit.
    Gene3Di2.60.120.200. 1 hit.
    3.90.1350.10. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    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.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 52 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

    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.