ALT11_ALTAL
ID ALT11_ALTAL Reviewed; 302 AA.
AC A0A3G9HRC8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Dioxygenase ALT11 {ECO:0000250|UniProtKB:Q8J2Q9};
DE EC=1.14.11.- {ECO:0000250|UniProtKB:W7LKX6};
DE AltName: Full=AAL-toxin biosynthesis cluster protein 11 {ECO:0000303|Ref.1};
GN Name=ALT11b {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: Dioxygenase; 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;
CC Evidence={ECO:0000250|UniProtKB:A0A097ZPD9};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:Q8J2Q9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WAW9}.
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 PhyH family. {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; BBG74284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9HRC8; -.
DR SMR; A0A3G9HRC8; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..302
FT /note="Dioxygenase ALT11"
FT /id="PRO_0000449863"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
SQ SEQUENCE 302 AA; 32979 MW; 41EE2A4F3A177549 CRC64;
MSSPELPSQM GVPNGHTKLQ EVTPDTPLDE VFQKWEEDGG VIIKGILAPA QVTQLREELQ
PLLDTFQRGS TTDIEPLKRF HGSQTKRAGG LTNCSAIFRD YLLDNDFLHA IAARCFGSGG
RPGVHAYWIS SANTINVGPG QPAQVLHRDL GNYPHYHLLG PDGPESQATF LIATTDFTDA
NGATRIIPGS QKWPFNQTWN PSQSIPSEMH AGDCLLFGGK VVHGTGANTT NAERGCVAFT
FCANHLTPEE AHPHIVDINI VRKLSERAQR SLGFRSQYPR GAPGLWMEGY NEVATRLGLD
SK
