BET3_NEOBT
ID BET3_NEOBT Reviewed; 364 AA.
AC A0A0C6DWS6;
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=Trans-enoyl reductase bet3 {ECO:0000303|PubMed:25530455};
DE EC=1.-.-.- {ECO:0000269|PubMed:25530455};
DE AltName: Full=Betaenone biosynthesis cluster protein 3 {ECO:0000303|PubMed:25530455};
GN Name=bet3 {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: Trans-enoyl reductase; part of the gene cluster that mediates
CC the biosynthesis of betaenones, phytotoxic polyketides involved in leaf
CC spot disease in sugar beets (PubMed:25530455). The first step of the
CC pathway is the synthesis of dehydroprobetaenone I by the polyketide
CC synthase bet1 and the enoyl reductase bet3 via condensation of one
CC acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations
CC (PubMed:25530455). The C-terminal reductase (R) domain of bet1
CC 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=acetyl-CoA + 10 AH2 + 2 H(+) + 7 malonyl-CoA + 5 S-adenosyl-L-
CC methionine = 10 A + 7 CO2 + 8 CoA + dehydroprobetaenone I + 6 H2O + 5
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51348, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:145061; Evidence={ECO:0000269|PubMed:25530455};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51349;
CC Evidence={ECO:0000269|PubMed:25530455};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25530455}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; LC011911; BAQ25464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C6DWS6; -.
DR SMR; A0A0C6DWS6; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..364
FT /note="Trans-enoyl reductase bet3"
FT /id="PRO_0000448654"
FT BINDING 53..56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 139..146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 174..177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 197..200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 263..264
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 283..287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 353..354
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 364 AA; 38107 MW; AF44D0274990CED8 CRC64;
MPPTNGQTAI IQSKTCPTPT TLPLVVAHGR PLPPLPSSHH VRVRVLAVGL NPTDHKMVTH
FFMQDNTTGC DFCGIIEEVG SASALPLGLR VCGADFPYRP SNPYNGAFAE YAVADSRHLL
QIPDAISNIQ AAAIGAIGWG TAALAMSDPT ALNLPGTPSK PDARSLPVLV YGGATATGII
AIQMLKRSGY IPIAVCSAQS APLCISLGAV GTACYTSTTC VQDIKALANG QSIKHALDCI
TDPESTTVCL ASLARIGGRY ACLEAVSDAC ITRRSVAVKV VMGFEGQNFD VDLGHPVYSR
KANPALHAVA AQWAAELQPL LNAGIIKTQP LEEIEGRFEG VIKALEMLQG GHIKGKKLVV
NISS
