ID   ALT3_ALTAL              Reviewed;         384 AA.
AC   A0A3G9HPE6;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Dehydrogenase ALT3 {ECO:0000250|UniProtKB:W7LUF3};
DE            EC=1.14.11.- {ECO:0000250|UniProtKB:W7LUF3};
DE   AltName: Full=AAL-toxin biosynthesis cluster protein 3 {ECO:0000303|Ref.1};
GN   Name=ALT3 {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: Dehydrogenase; part of the gene cluster that mediates the
CC       biosynthesis of the host-selective toxins (HSTs) AAL-toxins,
CC       sphinganine-analog mycotoxins responsible for Alternaria stem canker on
CC       tomato by the tomato pathotype (PubMed:18435561, PubMed:19749175,
CC       PubMed:19449880). The biosynthesis starts with the polyketide synthase
CC       ALT1-catalyzed C-16 carbon chain assembly from one starter acetyl-CoA
CC       unit with malonyl-CoA extender units (PubMed:18435561,
CC       PubMed:19449880). ALT1 also selectively transfers methyl groups at the
CC       first and the third cycle of chain elongation for AAL toxin
CC       (PubMed:19449880). The C-16 polyketide chain is released from the
CC       enzyme by a nucleophilic attack of a carbanion, which is derived from
CC       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=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:W7LUF3}.
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 iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AB969680; BBG74269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G9HPE6; -.
DR   SMR; A0A3G9HPE6; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   PANTHER; PTHR11496; PTHR11496; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
PE   3: Inferred from homology;
KW   Iron; NAD; Oxidoreductase.
FT   CHAIN           1..384
FT                   /note="Dehydrogenase ALT3"
FT                   /id="PRO_0000449852"
SQ   SEQUENCE   384 AA;  41252 MW;  5F0F20F3D53CF499 CRC64;
     MFGSLRTYIV SSKSISATPA FEALESALGT AKIAGIRCGI TSHSPWEDVF QLAQDIQATD
     ADLIITLGGC SITDAVKLAK LFIPNNVSTI PGAEELFARI RADESVKPAT IPVINVPTTL
     SGSEFTCAGG ATNLTTGHKQ VTMHSSLYAD VVVLDPRLSI STPRQVWLAT GVRAIDHFVE
     GLYGNVAALF TDMREELGNE ANEDIEKVIA GALGSLLTSL LSTKENWNDE EARLQAFLAV
     KECPRAGHNG IGASHGIGHQ LGPLGVGHGE TSCIILPWVL RYNWQHGDET ARRRLGLAID
     TFWGQEKVAE TLGATGLSRK DADLYDVVGA YISALGLPRT LGQFDIKEEQ LEGLAESAMK
     DWCTKVNPVT LTKDKVLDIL RNAK