TOXPH_AMAPH
ID TOXPH_AMAPH Reviewed; 143 AA.
AC D2KKB4;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Cytotoxic L-amino-acid oxidase {ECO:0000303|PubMed:20121947};
DE EC=1.4.3.2 {ECO:0000269|PubMed:20121947};
DE AltName: Full=Toxophallin {ECO:0000303|PubMed:20121947};
DE Flags: Fragment;
OS Amanita phalloides (Death cap).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX NCBI_TaxID=67723;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY,
RP AND FUNCTION.
RC TISSUE=Fruiting body;
RX PubMed=20121947; DOI=10.1111/j.1742-4658.2010.07557.x;
RA Stasyk T., Lutsik-Kordovsky M., Wernstedt C., Antonyuk V., Klyuchivska O.,
RA Souchelnytskyi S., Hellman U., Stoika R.;
RT "A new highly toxic protein isolated from the death cap Amanita phalloides
RT is an L-amino acid oxidase.";
RL FEBS J. 277:1260-1269(2010).
CC -!- FUNCTION: Cytotoxic L-amino acid oxidase with high oxidase activity
CC towards DL-methionine and L-methionine, L-phenylalanine, DL-norleucine,
CC L-isoleucine, L-arginine, L-tyrosine, and DL-leucine. Shows relatively
CC low activity towards DL-lysine and L-lysine, DL-asparagine, DL-valine,
CC L-histidine, DL-threonine, DL-thryptophane, and L-glutamic acid; and no
CC activity towards L-cysteine, L-glycine, L-proline, L-oxyproline, DL-
CC serine, and DL-aspartic acid. Does not use benzylamine, ethanolamine,
CC diethylamine, meta- and para-phenylendiamine, ortho-, meta- and para-
CC aminophenols, or putrescin as a substrate. Acts as a toxin by inducing
CC chromatin condensation, as well as DNA and nucleus fragmentation, which
CC are typical for apoptosis (PubMed:20121947). Probably induces cell
CC damage indirectly via the generation of free radicals and oxidant
CC agents that can trigger cell impairment and apoptosis by a caspase-
CC independent pathway (PubMed:20121947). {ECO:0000269|PubMed:20121947}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59869; EC=1.4.3.2;
CC Evidence={ECO:0000269|PubMed:20121947};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- MISCELLANEOUS: Ascorbic acid inhibits the cytotoxic effect caused by
CC toxophallin (PubMed:20121947). The mechanisms of such inhibition could
CC be based on inactivating the H(2)O(2) that appears as a result of the
CC amine oxidase reaction and is toxic for cells (PubMed:20121947).
CC {ECO:0000269|PubMed:20121947}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; GU220069; ADA58360.1; -; mRNA.
DR AlphaFoldDB; D2KKB4; -.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Toxin.
FT CHAIN <1..>143
FT /note="Cytotoxic L-amino-acid oxidase"
FT /id="PRO_0000443561"
FT NON_TER 1
FT /evidence="ECO:0000305"
FT NON_TER 143
FT /evidence="ECO:0000305"
SQ SEQUENCE 143 AA; 16087 MW; 5D91CA7EDFF0581B CRC64;
RVFHLFDYPP LNTGDLQLKA KIKPFIFTSN NSFLSYNDVT VKHNDVPAGD PFKASAVIKD
TNPNPYIAAG VTAILNDVLG RFAVPLMNDL KTGKTDGWDL MMKYDKHSTR SYMALAYTPS
DHLNLPKKPL PTDVINWLET FDK
