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VER1_DOTSE
ID   VER1_DOTSE              Reviewed;         263 AA.
AC   Q8TFD5;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Versicolorin reductase 1 {ECO:0000303|PubMed:23207690};
DE            Short=VER-1 {ECO:0000303|PubMed:23207690};
DE            EC=1.1.-.- {ECO:0000305|PubMed:23207690};
DE   AltName: Full=Dothistromin biosynthesis protein A {ECO:0000303|PubMed:12039746};
GN   Name=ver1 {ECO:0000303|PubMed:23207690};
GN   Synonyms=dotA {ECO:0000303|PubMed:12039746};
OS   Dothistroma septosporum (Red band needle blight fungus) (Mycosphaerella
OS   pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX   NCBI_TaxID=64363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=NZE1 / ATCC MYA-605;
RX   PubMed=12039746; DOI=10.1128/aem.68.6.2885-2892.2002;
RA   Bradshaw R.E., Bhatnagar D., Ganley R.J., Gillman C.J., Monahan B.J.,
RA   Seconi J.M.;
RT   "Dothistroma pini, a forest pathogen, contains homologs of aflatoxin
RT   biosynthetic pathway genes.";
RL   Appl. Environ. Microbiol. 68:2885-2892(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=NZE7;
RX   PubMed=17683963; DOI=10.1016/j.fgb.2007.06.005;
RA   Zhang S., Schwelm A., Jin H., Collins L.J., Bradshaw R.E.;
RT   "A fragmented aflatoxin-like gene cluster in the forest pathogen
RT   Dothistroma septosporum.";
RL   Fungal Genet. Biol. 44:1342-1354(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NZE1 / ATCC MYA-605;
RA   Bradshaw R.E., Monahan B.J., Gillman C.J.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=16649078; DOI=10.1007/s11046-006-0240-5;
RA   Bradshaw R.E., Jin H., Morgan B.S., Schwelm A., Teddy O.R., Young C.A.,
RA   Zhang S.;
RT   "A polyketide synthase gene required for biosynthesis of the aflatoxin-like
RT   toxin, dothistromin.";
RL   Mycopathologia 161:283-294(2006).
RN   [5]
RP   INDUCTION.
RX   PubMed=18262779; DOI=10.1016/j.mycres.2007.03.018;
RA   Schwelm A., Barron N.J., Zhang S., Bradshaw R.E.;
RT   "Early expression of aflatoxin-like dothistromin genes in the forest
RT   pathogen Dothistroma septosporum.";
RL   Mycol. Res. 112:138-146(2008).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22069539; DOI=10.3390/toxins1020173;
RA   Bradshaw R.E., Feng Z., Schwelm A., Yang Y., Zhang S.;
RT   "Functional analysis of a putative dothistromin toxin MFS transporter
RT   gene.";
RL   Toxins 1:173-187(2009).
RN   [7]
RP   REVIEW ON FUNCTION, AND PATHWAY.
RX   PubMed=22069571; DOI=10.3390/toxins2112680;
RA   Schwelm A., Bradshaw R.E.;
RT   "Genetics of dothistromin biosynthesis of Dothistroma septosporum: an
RT   update.";
RL   Toxins 2:2680-2698(2010).
RN   [8]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=23207690; DOI=10.1016/j.fgb.2012.11.006;
RA   Chettri P., Ehrlich K.C., Cary J.W., Collemare J., Cox M.P.,
RA   Griffiths S.A., Olson M.A., de Wit P.J., Bradshaw R.E.;
RT   "Dothistromin genes at multiple separate loci are regulated by AflR.";
RL   Fungal Genet. Biol. 51:12-20(2013).
RN   [9]
RP   FUNCTION.
RX   PubMed=23448391; DOI=10.1111/nph.12161;
RA   Bradshaw R.E., Slot J.C., Moore G.G., Chettri P., de Wit P.J.,
RA   Ehrlich K.C., Ganley A.R., Olson M.A., Rokas A., Carbone I., Cox M.P.;
RT   "Fragmentation of an aflatoxin-like gene cluster in a forest pathogen.";
RL   New Phytol. 198:525-535(2013).
RN   [10]
RP   INDUCTION.
RX   PubMed=25986547; DOI=10.1016/j.funbio.2015.01.007;
RA   Chettri P., Ehrlich K.C., Bradshaw R.E.;
RT   "Regulation of the aflatoxin-like toxin dothistromin by AflJ.";
RL   Fungal Biol. 119:503-508(2015).
CC   -!- FUNCTION: Versicolorin reductase; part of the fragmented gene cluster
CC       that mediates the biosynthesis of dothistromin (DOTH), a polyketide
CC       toxin very similar in structure to the aflatoxin precursor,
CC       versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571,
CC       PubMed:23207690, PubMed:23448391). The first step of the pathway is the
CC       conversion of acetate to norsolorinic acid (NOR) and requires the fatty
CC       acid synthase subunits hexA and hexB, as well as the polyketide
CC       synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a
CC       hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize
CC       the precursor NOR (By similarity). The hexanoyl starter unit is
CC       provided to the acyl-carrier protein (ACP) domain by the fungal fatty
CC       acid synthase hexA/hexB (By similarity). The second step is the
CC       conversion of NOR to averantin (AVN) and requires the norsolorinic acid
CC       ketoreductase nor1, which catalyzes the dehydration of norsolorinic
CC       acid to form (1'S)-averantin (PubMed:23207690). The cytochrome P450
CC       monooxygenase avnA then catalyzes the hydroxylation of AVN to
CC       5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed
CC       by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690).
CC       Averufin might then be converted to hydroxyversicolorone by cypX and
CC       avfA (PubMed:23207690). Hydroxyversicolorone is further converted
CC       versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is
CC       then the substrate for the versiconal hemiacetal acetate esterase est1
CC       to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase
CC       vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran
CC       ring (PubMed:16649078, PubMed:23207690). Then, the activity of the
CC       versicolorin B desaturase verB leads to versicolorin A (VERA)
CC       (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform
CC       epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a
CC       cytochrome P450, such as cypX or avnA could catalyze this step
CC       (PubMed:23207690). It is also possible that another, uncharacterized,
CC       cytochrome P450 enzyme is responsible for this step (PubMed:23207690).
CC       Opening of the epoxide could potentially be achieved by the epoxide
CC       hydrolase epoA (PubMed:23207690). However, epoA seems not to be
CC       required for DOTH biosynthesis, but other epoxide hydrolases may have
CC       the ability to complement this hydrolysis (PubMed:23207690).
CC       Alternatively, opening of the epoxide ring could be achieved non-
CC       enzymatically (PubMed:23207690). The next step is the deoxygenation of
CC       ring A to yield the 5,8-dihydroxyanthraquinone which is most likely
CC       catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690).
CC       The last stages of DOTH biosynthesis are proposed to involve
CC       hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might
CC       have oxidative roles here (PubMed:23207690). An alternative possibility
CC       is that cytochrome P450 monoogenases such as avnA and cypX might
CC       perform these steps in addition to previously proposed steps
CC       (PubMed:23207690). {ECO:0000250|UniProtKB:P50161,
CC       ECO:0000269|PubMed:12039746, ECO:0000269|PubMed:16649078,
CC       ECO:0000303|PubMed:22069571, ECO:0000305|PubMed:17683963,
CC       ECO:0000305|PubMed:23207690, ECO:0000305|PubMed:23448391}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000303|PubMed:22069571,
CC       ECO:0000305|PubMed:23207690}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P50161}.
CC   -!- INDUCTION: Expression is positively regulated by the dothistromin-
CC       specific transcription factors aflR and aflJ (PubMed:23207690,
CC       PubMed:25986547). Dothistromin biosynthetic proteins are co-regulated,
CC       showing a high level of expression at ealy exponential phase with a
CC       subsequent decline in older cultures (PubMed:17683963,
CC       PubMed:18262779). {ECO:0000269|PubMed:17683963,
CC       ECO:0000269|PubMed:18262779, ECO:0000269|PubMed:23207690,
CC       ECO:0000269|PubMed:25986547}.
CC   -!- DISRUPTION PHENOTYPE: Blocks the production of dothistromin and
CC       accumulates versicolorin A (PubMed:12039746).
CC       {ECO:0000269|PubMed:12039746}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF448056; AAL87045.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TFD5; -.
DR   SMR; Q8TFD5; -.
DR   OMA; ITGGRNW; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN           1..263
FT                   /note="Versicolorin reductase 1"
FT                   /id="PRO_0000443452"
FT   ACT_SITE        159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         15..43
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P16544"
FT   BINDING         163
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P16544"
SQ   SEQUENCE   263 AA;  27777 MW;  C647E756CBDF3CB7 CRC64;
     MSVDNFRLDG KVALVTGSGR GIGAAIAIEL GKRGANVVVN YSRAVAEANK VVETIIANGT
     KAIAIKADVG EIDQVAKMMD QAVEHFGQLD IVSSNAGLVS FGHLKDVTGD EFDRVFRVNT
     RGQFFVAREA YRHLSVGGRI ILTSSNTASI KGVPKHAIYS GSKGAIDTFV RCMAIDAGDK
     KITVNAVAPG AIKTDMYAAV AREYIPGGDK FTDEQVDECA AWLSPLERVG LPADIGRVVC
     FLASDAAEWV SGKILGIDGG AFR
 
 
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