ID   BET4_NEOBT              Reviewed;         346 AA.
AC   A0A0C6DRT7;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Short-chain dehydrogenase/reductase bet4 {ECO:0000303|PubMed:25530455};
DE            EC=1.1.1.- {ECO:0000305|PubMed:25530455};
DE   AltName: Full=Betaenone biosynthesis cluster protein 4 {ECO:0000303|PubMed:25530455};
GN   Name=bet4 {ECO:0000303|PubMed:25530455};
OS   Neocamarosporium betae (Beet black rot fungus) (Pleospora betae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Neocamarosporium.
OX   NCBI_TaxID=1979465;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RX   PubMed=25530455; DOI=10.1039/c4cc09512j;
RA   Ugai T., Minami A., Fujii R., Tanaka M., Oguri H., Gomi K., Oikawa H.;
RT   "Heterologous expression of highly reducing polyketide synthase involved in
RT   betaenone biosynthesis.";
RL   Chem. Commun. (Camb.) 51:1878-1881(2015).
CC   -!- FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster
CC       that mediates the biosynthesis of betaenones, phytotoxic polyketides
CC       involved in leaf spot disease in sugar beets (PubMed:25530455). The
CC       first step of the pathway is the synthesis of dehydroprobetaenone I by
CC       the polyketide synthase bet1 and the enoyl reductase bet3 via
CC       condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units
CC       and 5 methylations (PubMed:25530455). The C-terminal reductase (R)
CC       domain of bet1 catalyzes the reductive release of the polyketide chain
CC       (PubMed:25530455). Because bet1 lacks a designated enoylreductase (ER)
CC       domain, the required activity is provided the enoyl reductase bet3
CC       (PubMed:25530455). The short-chain dehydrogenase/reductase bet4 then
CC       catalyzes reduction of dehydroprobetaenone I to probetaenone I
CC       (PubMed:25530455). The cytochrome P450 monooxygenase bet2 catalyzes
CC       successive epoxidation, oxidation (resulting from epoxide opening) and
CC       hydroxylation to install a tertiary alcohol in the decaline ring to
CC       yield betaenone C from dehydroprobetaenone I and betaenone B from
CC       probetaenone I (PubMed:25530455). The FAD-linked oxidoreductase (orf1)
CC       is probably responsible for the conversion of betaenone C to betaenone
CC       A via an intramolecular aldol reaction between C-1 and C-17 to form the
CC       bridged tricyclic system in betaenone A (By similarity).
CC       {ECO:0000250|UniProtKB:Q0UK53, ECO:0000269|PubMed:25530455}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + dehydroprobetaenone I = A + probetaenone I;
CC         Xref=Rhea:RHEA:61864, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:145061, ChEBI:CHEBI:145062;
CC         Evidence={ECO:0000269|PubMed:25530455};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61865;
CC         Evidence={ECO:0000269|PubMed:25530455};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25530455}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; LC011911; BAQ25463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C6DRT7; -.
DR   SMR; A0A0C6DRT7; -.
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   1: Evidence at protein level;
KW   NAD; NADP; Oxidoreductase.
FT   CHAIN           1..346
FT                   /note="Short-chain dehydrogenase/reductase bet4"
FT                   /id="PRO_0000448656"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        222
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         48..56
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         75..76
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         111..113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         222..226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         255..257
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
SQ   SEQUENCE   346 AA;  37160 MW;  598A9C2FC782AB39 CRC64;
     MTPAKAPSHA KKPEAGSQPI SSMWTQMFPP KPTYTEEHMP DLSGKIYIVT GASSGVGKET
     SRMLYSKNAK VYMAMRSGAK AAAAMADIQR AVPKSSGALV ILPLDLADLS AVKKAAEEFV
     SLESSLHGLI NNAGVQVLDD TNGEARTAQG HEIHIGVNVL GPFLFTQLLR GVLAATAGRA
     QPDTVRIVWV SSMGTETIGE KGRGLSADYV DYWPLMSPLE RYGLSKAGNW LQGAECAKRY
     AGDGILSFPI NPGHLKSELY REGGTLFKLA LRPVLFPPAY GSYVELFAAL SPTLSTKDSG
     AWIVPWGRLY PIRSDLLDAT KSAAEGGNGH ASAFWDWCEE QVKAFL