ALT8_ALTAL
ID ALT8_ALTAL Reviewed; 599 AA.
AC A0A3G9HB50;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Cytochrome P450 monooxygenase ALT8 {ECO:0000250|UniProtKB:W7LC91};
DE EC=1.-.-.- {ECO:0000250|UniProtKB:W7LC91};
DE AltName: Full=AAL-toxin biosynthesis cluster protein 8 {ECO:0000303|Ref.1};
GN Name=ALT8 {ECO:0000303|Ref.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=As-27;
RA Akagi Y., Akamatsu H., Takao K., Tsuge T., Kodama M.;
RT "AAL-toxin biosynthetic genes cluster in the tomato pathotype of Alternaria
RT alternata.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=18435561; DOI=10.1021/np8000514;
RA Zhu X., Vogeler C., Du L.;
RT "Functional complementation of fumonisin biosynthesis in FUM1-disrupted
RT fusarium verticillioides by the AAL-toxin polyketide synthase gene ALT1
RT from Alternaria alternata f. sp. Lycopersici.";
RL J. Nat. Prod. 71:957-960(2008).
RN [3]
RP FUNCTION.
RX PubMed=19749175; DOI=10.1128/ec.00135-09;
RA Akagi Y., Akamatsu H., Otani H., Kodama M.;
RT "Horizontal chromosome transfer, a mechanism for the evolution and
RT differentiation of a plant-pathogenic fungus.";
RL Eukaryot. Cell 8:1732-1738(2009).
RN [4]
RP FUNCTION.
RX PubMed=19449880; DOI=10.1021/np900193j;
RA Li Y., Shen Y., Zhu X., Du L.;
RT "Introduction of the AAL-toxin polyketide synthase gene ALT1 into FUM1-
RT disrupted Fusarium verticillioides produces metabolites with the fumonisin
RT methylation pattern.";
RL J. Nat. Prod. 72:1328-1330(2009).
RN [5]
RP FUNCTION.
RX DOI=10.4172/2157-7471.S2-001;
RA Kheder A.A., Akagi Y., Tsuge T., Kodama M.;
RT "Functional analysis of the ceramide synthase gene ALT7, a homolog of the
RT disease resistance gene Asc1, in the plant pathogen Alternaria alternata.";
RL J. Plant Pathol. Microbiol. 2:0-0(2012).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the host-selective toxins (HSTs) AAL-
CC toxins, sphinganine-analog mycotoxins responsible for Alternaria stem
CC canker on tomato by the tomato pathotype (PubMed:18435561,
CC PubMed:19749175, PubMed:19449880). The biosynthesis starts with the
CC polyketide synthase ALT1-catalyzed C-16 carbon chain assembly from one
CC starter acetyl-CoA unit with malonyl-CoA extender units
CC (PubMed:18435561, PubMed:19449880). ALT1 also selectively transfers
CC methyl groups at the first and the third cycle of chain elongation for
CC AAL toxin (PubMed:19449880). The C-16 polyketide chain is released from
CC the enzyme by a nucleophilic attack of a carbanion, which is derived
CC from R-carbon of glycin by decarboxylation, on the carbonyl carbon of
CC polyketide acyl chain (Probable). This step is probably catalyzed by a
CC pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable).
CC The respective functions of the other enzymes encoded by the cluster
CC have still to be elucidated (Probable). The sphingosine N-
CC acyltransferase-like protein ALT7 seems not to act as a
CC resistance/self-tolerance factor against the toxin in the toxin
CC biosynthetic gene cluster, contrary to what is expected (Ref.5).
CC {ECO:0000269|PubMed:18435561, ECO:0000269|PubMed:19449880,
CC ECO:0000269|PubMed:19749175, ECO:0000269|Ref.5,
CC ECO:0000305|PubMed:19449880}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000250|UniProtKB:W7LC91}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Gene clusters encoding host-selective toxins (HSTs) are
CC localized on conditionally dispensable chromosomes (CDCs), also called
CC supernumerary chromosomes, where they are present in multiple copies.
CC The CDCs are not essential for saprophytic growth but controls host-
CC selective pathogenicity. {ECO:0000269|PubMed:19749175}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB969680; BBG74272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9HB50; -.
DR SMR; A0A3G9HB50; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..599
FT /note="Cytochrome P450 monooxygenase ALT8"
FT /id="PRO_0000449851"
FT TRANSMEM 4..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 495..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 539
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 599 AA; 66513 MW; 165A73481F5587E6 CRC64;
MATLACVGAA AMACALAVYL GDTTKSMSYL SYSGTILFGC SGLWYVWKGL LWPAYFSPLR
HLKTVPKSGW LSAETLRLYT EPRGVPQCEW INKLDSVPQG LVRYRSILGF ERLLVVSPEA
LADVLVNRSY EFQKPAFVVT QLEQILGRGV LLAEGNEHRA QRRVLLPAFA FRHVKSLYPV
MWSVAEHLIT SMTENIRVES SASPTEPVFS SDEPQAKHKH EMITVNIADL CSRATLDIIG
IAGIGQEFGA IRNPNNALHQ TYCEIFQPSK EATLLGVLRL LLPIWFVDWL PSRRNARVQR
AVQTIRSLCR QIIQEERLPQ AVDESHSEVA STGKNILTLA IASGAFTDEA LVDQIMTFLA
AGHETTATAL TWAIYIMCLH PGIQEKLRNE VRSRLPKLPS TYNSAPQNLA KTIDTGMPYL
NAVCQEVFRY FPPIPVTFRE ATKNTFILNT AVPAGTKIVL APRVTNRQST LWGSNAQEFD
PDRWLCLKKQ DASIDDSSAA SPSFGGSGKR KSQYTDTHKE PSTRSNFATM TFLHGPRSCI
GQSFAKAELA ILLAALVGRF EFKLARGTPE KEIDVRVSRG ATARPEKGLF VQIRVIEGW
