ID   DPCHG_COLHI             Reviewed;         268 AA.
AC   H1VN83;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Short chain dehydrogenase/reductase dpchG {ECO:0000303|PubMed:32286350};
DE            EC=1.1.1.- {ECO:0000269|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein G {ECO:0000303|PubMed:32286350};
GN   Name=dpchG {ECO:0000303|PubMed:32286350};
GN   ORFNames=CH063_11894, CH63R_05477;
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063;
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063;
RA   O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT   "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOTECHNOLOGY.
RX   PubMed=32286350; DOI=10.1038/s41467-020-15664-4;
RA   Tsukada K., Shinki S., Kaneko A., Murakami K., Irie K., Murai M.,
RA   Miyoshi H., Dan S., Kawaji K., Hayashi H., Kodama E.N., Hori A., Salim E.,
RA   Kuraishi T., Hirata N., Kanda Y., Asai T.;
RT   "Synthetic biology based construction of biological activity-related
RT   library of fungal decalin-containing diterpenoid pyrones.";
RL   Nat. Commun. 11:1830-1830(2020).
CC   -!- FUNCTION: Short chain dehydrogenase/reductase; part of the gene cluster
CC       that mediates the biosynthesis of the diterpenoid pyrones higginsianins
CC       A and B (PubMed:32286350). The first step of the pathway is the
CC       synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA
CC       via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA
CC       units and 2 methylations (Probable). The alpha-pyrone is then combined
CC       with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase
CC       dpchD through the action of the prenyltransferase dpchC to yield a
CC       linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the
CC       diterpenoid pyrone biosynthetic pathway involve the decalin core
CC       formation, which is initiated by the epoxidation of the C10-C11 olefin
CC       by the FAD-dependent oxidoreductase dpchE, and is followed by a
CC       cyclization cascade catalyzed by the terpene cyclase dpchB (Probable).
CC       The short chain dehydrogenase/reductase dpchG then oxidizes the 8S
CC       hydroxy group to a ketone and the short chain dehydrogenase/reductase
CC       dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin
CC       B (PubMed:32286350). Finally, the FAD-dependent oxidoreductase dpchF
CC       converts higginsianin B into higginsianin A (PubMed:32286350).
CC       {ECO:0000269|PubMed:32286350, ECO:0000305|PubMed:32286350}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:32286350}.
CC   -!- BIOTECHNOLOGY: Diterpenoid pyrones display various biological
CC       activities and higginsianin A shows anti-HIV activity.
CC       {ECO:0000269|PubMed:32286350}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CACQ02004858; CCF41687.1; -; Genomic_DNA.
DR   EMBL; LTAN01000004; OBR09785.1; -; Genomic_DNA.
DR   RefSeq; XP_018158302.1; XM_018300452.1.
DR   AlphaFoldDB; H1VN83; -.
DR   SMR; H1VN83; -.
DR   STRING; 80884.CCF41687; -.
DR   EnsemblFungi; CCF41687; CCF41687; CH063_11894.
DR   GeneID; 28864559; -.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_1_0_1; -.
DR   OrthoDB; 1226147at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   Proteomes; UP000092177; Chromosome 4.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..268
FT                   /note="Short chain dehydrogenase/reductase dpchG"
FT                   /id="PRO_0000451549"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         44
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         70..71
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         97
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
SQ   SEQUENCE   268 AA;  27687 MW;  16EF74BB6E672EA1 CRC64;
     MTSSEKNSTG LAGKTCLVTG GAGGLGKAVT AAFLDAGANV VICDINAKRI ESTLAELRTR
     GGNLTAVTAD ITDHDQVLSL FDDIAGRFGT LDVLVNNAAV MDRFDPVGDI ELDLWDNVLA
     VNLTAPLQLS KFAVRSMLSK PEPAGCIINI ASGAATAGWL AGTAYTASKH GLVGLTKSTA
     AFYGPKGIRC NALIMGVMVG THMHEAFLDG CHKEGRQKVE EIFSGHRPQT CKVDDVAGIC
     LSLASGPGWG TVNGALIAVD NGWTSVVG