ALT6_ALTAL
ID ALT6_ALTAL Reviewed; 354 AA.
AC A0A3G9HN61;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=NAD-dependent epimerase/dehydratase ALT6 {ECO:0000250|UniProtKB:W7LL82};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:W7LL82};
DE AltName: Full=AAL-toxin biosynthesis cluster protein 6 {ECO:0000303|Ref.1};
GN Name=ALT6 {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: NAD-dependent epimerase/dehydratase; part of the gene cluster
CC that 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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:W7LL82}.
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 NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB969680; BBG74268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9HN61; -.
DR SMR; A0A3G9HN61; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Oxidoreductase.
FT CHAIN 1..354
FT /note="NAD-dependent epimerase/dehydratase ALT6"
FT /id="PRO_0000449859"
FT BINDING 41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
SQ SEQUENCE 354 AA; 38409 MW; DAA29F6A26F3B214 CRC64;
MDNERRLVLL TGATGHVGFA VLVEALEAEY NVRVVLREIS KADSILSSEP VKNALSSTAA
PELSFVEVPD MTVPGAFDSA MQSVTYVVHC ASPINRGKFR DFQTELIDPA VKGTTNILKA
AHATPSVLRV VITSSNSAIV NHNILPAPGT CVSPSDRQPD YPLDVAMHDA DEAYSAAKTS
ALNATDTFVS SANDLRFDVV SIMPTFVFGP KELAKSPGDI IDGSNVFGIG LVLIKQSWGS
LRIEAVSCHI DDVAQAHVQA LNHDEDVQFP FKAGTHRSCL LASSFRPDEV RDIVEREFPK
ESWQGEEAVF RGKGSYAWYH TDYDVSAAEK LLGRKLKGIV EQIRSSGLQV LRIA
