ALT7_ALTAL
ID ALT7_ALTAL Reviewed; 432 AA.
AC G1UJF5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Sphingosine N-acyltransferase-like protein ALT7 {ECO:0000303|Ref.6};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:W7LKY5};
DE AltName: Full=AAL-toxin biosynthesis cluster protein 7 {ECO:0000303|Ref.6};
GN Name=ALT7 {ECO:0000303|Ref.6};
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 Kheder A., Akagi Y., Kodama M.;
RT "Functional analysis of ALT7.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP DISRUPTION PHENOTYPE, AND 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: Sphingosine N-acyltransferase-like protein; part of the gene
CC cluster that mediates the biosynthesis of the host-selective toxins
CC (HSTs) AAL-toxins, sphinganine-analog mycotoxins responsible for
CC Alternaria stem canker on tomato by the tomato pathotype
CC (PubMed:18435561, PubMed:19749175, PubMed:19449880). The biosynthesis
CC starts with the polyketide synthase ALT1-catalyzed C-16 carbon chain
CC assembly from one starter acetyl-CoA unit with malonyl-CoA extender
CC units (PubMed:18435561, PubMed:19449880). ALT1 also selectively
CC transfers methyl groups at the first and the third cycle of chain
CC elongation for AAL toxin (PubMed:19449880). The C-16 polyketide chain
CC is released from the enzyme by a nucleophilic attack of a carbanion,
CC which is derived from R-carbon of glycin by decarboxylation, on the
CC carbonyl carbon of polyketide acyl chain (Probable). This step is
CC probably catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl
CC transferase ALT4 (Probable). The respective functions of the other
CC enzymes encoded by the cluster have still to be elucidated (Probable).
CC The sphingosine N-acyltransferase-like protein ALT7 seems not to act as
CC a resistance/self-tolerance factor against the toxin in the toxin
CC biosynthetic gene cluster, contrary to what is expected (Ref.6).
CC {ECO:0000269|PubMed:18435561, ECO:0000269|PubMed:19449880,
CC ECO:0000269|PubMed:19749175, ECO:0000269|Ref.6,
CC ECO:0000305|PubMed:19449880}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Does not cause any detectable defects in the
CC vegetative and reproductive properties of the toxin-producing pathogen.
CC The deletion of ALT7 has no deleterious effect on the toxin-producing
CC pathogen, indicating that the gene does not act as a resistance/self-
CC tolerance factor against the toxin in the toxin biosynthetic gene
CC cluster. {ECO:0000269|Ref.6}.
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 sphingosine N-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB666460; BAK64384.1; -; Genomic_DNA.
DR EMBL; AB969680; BBG74271.1; -; Genomic_DNA.
DR AlphaFoldDB; G1UJF5; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0046513; P:ceramide biosynthetic process; IEA:InterPro.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR InterPro; IPR013599; TRAM1.
DR PANTHER; PTHR12560; PTHR12560; 1.
DR Pfam; PF08390; TRAM1; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..432
FT /note="Sphingosine N-acyltransferase-like protein ALT7"
FT /id="PRO_0000449860"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 123..366
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 370..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 432 AA; 49152 MW; 00478D57491DE709 CRC64;
MFRPDLDDIP ALGSETSSLD NTVENGNYRV KLWRDKSGIR SPPSTFCTWF KQYQIGLSLG
SLLLLILMFT CLPYYDNVSG TYTRGRDDLA FIFSGVVLFT ALRAISMIYL LEPLARLCGV
HKKLMVRFTE QGWLVIHHSL FWTTGMYINY NSEYWMDLDG VWSGFPERTM TGLTKGYYLL
QLAFWLQQIV VVNFEKRRKD YSQMLTHHLI TSVLLATSYS YYQTKVGNVI LCLVDIVDVL
FAFAKLLKYL GFQYACDVAF CVFLASWLVA RHGLYLLVCW SIFTILPTVM PYGCYDTISG
NRLSEFPADG GNEIMREVLQ AFRDPGGPVC FNSRIGWAFL GLLVGLQVLM LIWLGMILKV
AYKVFQGEGA DDTRSDSEES GYGTSDHEGD CYGAQAGNPK VIRQFVASRE KVHIEQAENQ
GLHLRQQKRS AR
