ID   ALT12_ALTAL             Reviewed;         554 AA.
AC   A0A3G9H9H8;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 2.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Nonribosomal peptide synthetase ALT12 {ECO:0000250|UniProtKB:Q8J2Q9};
DE            EC=6.3.2.- {ECO:0000250|UniProtKB:Q8J2Q6};
DE   AltName: Full=AAL-toxin biosynthesis cluster protein 12 {ECO:0000303|Ref.1};
GN   Name=ALT12 {ECO:0000305};
GN   Synonyms=ALT12a {ECO:0000303|Ref.1}, ALT12b {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: Nonribosomal peptide synthetase; 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:Q8J2Q9}.
CC   -!- DOMAIN: ALT12 encodes a nonribosomal peptide synthetase containing two
CC       domains, a peptidyl carrier protein domain and a condensation domain.
CC       {ECO:0000250|UniProtKB:Q8J2Q6}.
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 NRP synthetase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BBG74275.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BBG74283.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB969680; BBG74275.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB969680; BBG74283.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A0A3G9H9H8; -.
DR   SMR; A0A3G9H9H8; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Ligase; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..554
FT                   /note="Nonribosomal peptide synthetase ALT12"
FT                   /id="PRO_0000449864"
FT   DOMAIN          1..76
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          124..434
FT                   /note="Condensation"
FT                   /evidence="ECO:0000250|UniProtKB:Q8J2Q6"
FT   MOD_RES         35
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   554 AA;  61721 MW;  4914624863A8FAF2 CRC64;
     MASLEHMKRI WGEVLGIEPD EIGLDENFVD LGGDSVGTKA LQLLGEVASY NVQIDLETFT
     NTGTIQTLWE AMNDTQTRNV HSMDGRDYNT DSEGLDVVEA ASASIVTKTD TDNDDLALEQ
     ARLVQDNVLC VAPISPVQGF FLDLGLAGQI GLINYIFEVE GSDLKHGLAH VTNLLESKNP
     VFRTLIEKTK ESGFVQILVA KTRSSWFYPS DLRLYLEKTM TQKFELGKPA VQYALVMEDA
     AHEGRNFFVI SMHHTHCDAF SRFLIGKEIS QILESPSYYA RSENIERPWF GNYVKHVQQK
     ATDDKASLFW DAYMCGANLA NIYPLHRATL NGEFDGAIIE KIQAPVATRI ADGSPRNSTQ
     VILAAWAIAL ANLSGLRDIT FGLCRHGRSS SSFRDVRRLM GPLVNVLPFR VSLICNEEPA
     PALLQRIQNE ITSTNKHEHG FSPCIFPSTD GRPWVQSLVD LKSELHGMGN GPSARSDHLA
     ISKMVPRPDL DTYEMKSHWA VLLSIRQHRN VFQVSMYYQK PLLAEGKAVV LFENFRACIQ
     ALSTGQNSVG ELLE