ID   SOL3_ALTSO              Reviewed;         285 AA.
AC   D7UQ42;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Short chain dehydrogenase sol3 {ECO:0000303|PubMed:20486243};
DE            EC=1.1.1.- {ECO:0000305|PubMed:20486243};
DE   AltName: Full=Solanapyrone biosynthesis protein 3 {ECO:0000303|PubMed:20486243};
GN   Name=sol3;
OS   Alternaria solani.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Porri.
OX   NCBI_TaxID=48100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=20486243; DOI=10.1002/cbic.201000173;
RA   Kasahara K., Miyamoto T., Fujimoto T., Oguri H., Tokiwano T., Oikawa H.,
RA   Ebizuka Y., Fujii I.;
RT   "Solanapyrone synthase, a possible Diels-Alderase and iterative type I
RT   polyketide synthase encoded in a biosynthetic gene cluster from Alternaria
RT   solani.";
RL   ChemBioChem 11:1245-1252(2010).
RN   [2]
RP   FUNCTION.
RX   PubMed=9659400; DOI=10.1016/s0167-4838(98)00040-5;
RA   Katayama K., Kobayashi T., Oikawa H., Honma M., Ichihara A.;
RT   "Enzymatic activity and partial purification of solanapyrone synthase:
RT   first enzyme catalyzing Diels-Alder reaction.";
RL   Biochim. Biophys. Acta 1384:387-395(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=18256508; DOI=10.1271/bbb.70600;
RA   Katayama K., Kobayashi T., Chijimatsu M., Ichihara A., Oikawa H.;
RT   "Purification and N-terminal amino acid sequence of solanapyrone synthase,
RT   a natural Diels-Alderase from Alternaria solani.";
RL   Biosci. Biotechnol. Biochem. 72:604-607(2008).
CC   -!- FUNCTION: Short chain dehydrogenase; part of the gene cluster that
CC       mediates the biosynthesis of the phytotoxin solanapyrone, a causal
CC       agent of early blight disease of potato and tomato (PubMed:20486243).
CC       The prosolanapyrone synthase sol1 is a polyketide synthase that
CC       produces the octaketide desmethylprosolanapyrone I via sequential
CC       condensations of 7 malonyl-CoA units with one acetyl-CoA unit, and one
CC       methylation step (PubMed:20486243). The octaketide backbone is further
CC       methylated by the sol2 O-methyltransferase to yield prosolanapyrone I
CC       (PubMed:20486243). Prosolanapyrone I is hydroxylated to prosolanapyrone
CC       II by the cytochrome P450 monooxygenase sol6 (PubMed:20486243). The
CC       solanapyrone synthase sol5 then catalyzes the oxidation of
CC       prosolanapyrone II and the subsequent Diels Alder cycloisomerization of
CC       the product prosolanapyrone III to solanapyrones A and D
CC       (PubMed:9659400, PubMed:18256508). Solanapyrones A and D are then
CC       converted into solanapyrones B and E, respectively, by the sol3
CC       dehydrogenase (PubMed:20486243). {ECO:0000269|PubMed:18256508,
CC       ECO:0000269|PubMed:20486243, ECO:0000269|PubMed:9659400}.
CC   -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000305|PubMed:20486243}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AB514562; BAJ09787.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7UQ42; -.
DR   SMR; D7UQ42; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NAD; NADP; Oxidoreductase.
FT   CHAIN           1..285
FT                   /note="Short chain dehydrogenase sol3"
FT                   /id="PRO_0000438553"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         31..39
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         58..59
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         109..111
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         200..204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         232..234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
SQ   SEQUENCE   285 AA;  31165 MW;  326882835A4ACC13 CRC64;
     MGGMLGFFVR QLTFMPKPLP QNVRLDGKTA IVTGANVGLG LEASKEMASH GLARVILGVR
     TVSKGEAAKQ EILKQSPNCD VQVWPVDHES FESMVAFGER AQSLDRLDIV ILCAGVKNLV
     FSLSKTGHEQ NVQVNHLGTS LLSLLLLKPL KDTAAKTGSP SRLTIVASEV HFWTPFDERK
     APSILARLDE KDSFRGMERY NTSKLLNILW MRELSSRVTG NVVINAVNPG LCASALHRTD
     PTPGLAYLNK IFAWTPAQGG HNLTYAATQH VDEPGAYLSE QHLEK