ALT10_ALTAL
ID ALT10_ALTAL Reviewed; 566 AA.
AC A0A3G9H9I5;
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=Acyl-CoA synthetase ALT10 {ECO:0000250|UniProtKB:Q8J2Q9};
DE EC=6.2.1.- {ECO:0000250|UniProtKB:Q8J2R0};
DE AltName: Full=AAL-toxin biosynthesis cluster protein 10 {ECO:0000303|Ref.1};
GN Name=ALT10 {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: Acyl-CoA synthetase; part of the gene cluster that mediates
CC the 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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:Q8J2Q9}.
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 ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB969680; BBG74285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9H9I5; -.
DR SMR; A0A3G9H9I5; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding.
FT CHAIN 1..566
FT /note="Acyl-CoA synthetase ALT10"
FT /id="PRO_0000449862"
FT REGION 473..551
FT /note="AMP-binding"
FT /evidence="ECO:0000255"
FT BINDING 196..207
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
SQ SEQUENCE 566 AA; 61573 MW; C7EC2FE96BD8031C CRC64;
MTANVNVLVL PTHMRENDSA AIIIPSTRSA PQKEVSYKHL VAITDSLHRD LAHLGITKAC
KVAIVLPNGL EFVAVFLSVL RQRAVAAPLD AQLTESEFKD IFSRMKPELV IMLPIPPESS
GGPCLPAPAM RAALGLTLRV ALCRRTSDVK DGSGLGLQLA LDLLEPAHSN HPAVAIVPKA
SAYSRDDVWS EDGALMLFTS GTTGAPKSVV LSHINLLVAM RIIIANHQLS SMDRTIIITP
LHHIIGVCGS LLVTLFSGAC AVIPDSLPGA FWQYCTEFGV TWFHAVPTLH RLLLKFPRTK
DSMPPRLRFL RSGGSEMAPD LYETLKAFGV PVLEVYGMTE TGPAIFCNHL DENGAGARQR
SHYPIPDAVD VMILVSSDQP EGETYDKTSL QADQYSNLKM TKEPGVIGEV CVRGKNVMAG
YINNSRANTE AFLPNGYFRT GDLGTIQSSG QLKLVGRLKE VINKGGIKIG PSEVEHAALS
HESVSEAVCF RIADVMYGEE IGLAVKLRSN SGKNQCTDRD LKQHIRYQLS AFKVPKEIVF
VDAVHYNRTG KPLRTQVSQK FAEGLL
