ID   AMT16_ALTAL             Reviewed;         374 AA.
AC   C9K7C8;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase AMT16 {ECO:0000255|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000255|PIRNR:PIRNR001361};
DE   AltName: Full=AM-toxin biosynthesis protein 16 {ECO:0000303|PubMed:17990954};
GN   Name=AMT16 {ECO:0000303|PubMed:17990954};
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], INDUCTION, AND PATHWAY.
RC   STRAIN=NBRC 8984;
RX   PubMed=17990954; DOI=10.1094/mpmi-20-12-1463;
RA   Harimoto Y., Hatta R., Kodama M., Yamamoto M., Otani H., Tsuge T.;
RT   "Expression profiles of genes encoded by the supernumerary chromosome
RT   controlling AM-toxin biosynthesis and pathogenicity in the apple pathotype
RT   of Alternaria alternata.";
RL   Mol. Plant Microbe Interact. 20:1463-1476(2007).
RN   [2]
RP   FUNCTION.
RC   STRAIN=M-71;
RX   PubMed=10875335; DOI=10.1094/mpmi.2000.13.7.742;
RA   Johnson R.D., Johnson L., Itoh Y., Kodama M., Otani H., Kohmoto K.;
RT   "Cloning and characterization of a cyclic peptide synthetase gene from
RT   Alternaria alternata apple pathotype whose product is involved in AM-toxin
RT   synthesis and pathogenicity.";
RL   Mol. Plant Microbe Interact. 13:742-753(2000).
RN   [3]
RP   FUNCTION.
RC   STRAIN=NBRC 8984;
RX   PubMed=15066029; DOI=10.1111/j.1365-2958.2004.04004.x;
RA   Ito K., Tanaka T., Hatta R., Yamamoto M., Akimitsu K., Tsuge T.;
RT   "Dissection of the host range of the fungal plant pathogen Alternaria
RT   alternata by modification of secondary metabolism.";
RL   Mol. Microbiol. 52:399-411(2004).
RN   [4]
RP   REVIEW ON HOST-SELECTIVE TOXINS.
RX   PubMed=22846083; DOI=10.1111/j.1574-6976.2012.00350.x;
RA   Tsuge T., Harimoto Y., Akimitsu K., Ohtani K., Kodama M., Akagi Y.,
RA   Egusa M., Yamamoto M., Otani H.;
RT   "Host-selective toxins produced by the plant pathogenic fungus Alternaria
RT   alternata.";
RL   FEMS Microbiol. Rev. 37:44-66(2013).
CC   -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene clusters
CC       that mediate the biosynthesis of AM-toxins, host-selective toxins
CC       (HSTs) causing Alternaria blotch on apple, a worldwide distributed
CC       disease (Probable). AM-toxins are cyclic depsipeptides containing the 3
CC       residues 2-hydroxy-isovaleric acid (2-HIV), dehydroalanine, L-alanine
CC       which are common for all 3 AM-toxins I to III. The fourth precursor is
CC       L-alpha-amino-methoxyphenyl-valeric acid (L-Amv) for AM-toxin I, L-
CC       alpha-amino-phenyl-valeric acid (L-Apv) for AM-toxin II, and L-alpha-
CC       amino-hydroxyphenyl-valeric acid (L-Ahv) for AM-toxin III (Probable).
CC       AM-toxins have two target sites for affecting susceptible apple cells;
CC       they cause invagination of the plasma membrane and electrolyte loss and
CC       chloroplast disorganization (PubMed:22846083). The non-ribosomal
CC       peptide synthetase AMT1 contains 4 catalytic modules and is responsible
CC       for activation of each residue in AM-toxin (PubMed:10875335). The aldo-
CC       keto reductase AMT2 catalyzes the conversion of 2-keto-isovaleric acid
CC       (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV), one of the precursor
CC       residues incorporated by AMT1 during AM-toxin biosynthesis, by
CC       reduction of its ketone to an alcohol (PubMed:15066029). The cytochrome
CC       P450 monooxygenase AMT3 and the thioesterase AMT4 are also important
CC       for AM-toxin production, but their exact function within the AM-toxin
CC       biosynthesis are not known yet (PubMed:17990954). Up to 21 proteins
CC       (including AMT1 to AMT4) are predicted to be involved in AM-toxin
CC       biosynthesis since their expression ishighly up-regulated in AM-toxin-
CC       producing cultures (PubMed:17990954). {ECO:0000269|PubMed:10875335,
CC       ECO:0000269|PubMed:15066029, ECO:0000269|PubMed:17990954,
CC       ECO:0000303|PubMed:22846083, ECO:0000305|PubMed:10875335,
CC       ECO:0000305|PubMed:17990954}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC         phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC         Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC         Evidence={ECO:0000255|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:17990954}.
CC   -!- INDUCTION: Expression is up-regulated more than 10 fold in toxin
CC       producing cultures. {ECO:0000269|PubMed:17990954}.
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       (PubMed:17990954). The CDCs are not essential for saprophytic growth
CC       but controls host-selective pathogenicity (PubMed:17990954).
CC       {ECO:0000269|PubMed:17990954}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR   EMBL; AB525198; BAI44752.1; -; Genomic_DNA.
DR   EMBL; AB525199; BAI44773.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9K7C8; -.
DR   SMR; C9K7C8; -.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DHAP_synth_1.
DR   PANTHER; PTHR21225; PTHR21225; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Transferase;
KW   Virulence.
FT   CHAIN           1..374
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase AMT16"
FT                   /id="PRO_0000444866"
SQ   SEQUENCE   374 AA;  41150 MW;  5E3388A4934DD8BF CRC64;
     MSFHVNNKAV GDPLNSEDWR IKGYNPLTPP NLLQSEIPQT AKSRDTVFKA REEVIAIFQN
     KDAQKRLLVV IGPCSIHDPL AALEYCDRLM KLKEKYQDDL LIVMRSYLEK PRTTIGWKGL
     INDPDIDNSF KINKGLRISR QLFADLTEKG MPLASEMLDT ISPQFLADMF SVGVIGARTT
     ESQLHRELAS GLSFPVGFKN GTDGTLDVAI DAIDSAKYPH HFLSVTKPGV VAIVGTIGNH
     DCFIILRGGR KGTNYDAKSI KEAREKLESE GMNPRLMIDC SHGNSEKNHM NQPKVVHAVA
     EQIEAGETAV IGVMIESNLK AGTQKVPKEG KAGLEYGMSI TDACIDWKTT ETVLAELAGA
     VAKRRTLLGQ NGTY