DPCHH_COLHI
ID DPCHH_COLHI Reviewed; 401 AA.
AC A0A1B7YCL6; H1VQB2;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Short chain dehydrogenase/reductase dpchH {ECO:0000303|PubMed:32286350};
DE EC=1.1.1.- {ECO:0000269|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein H {ECO:0000303|PubMed:32286350};
GN Name=dpchH {ECO:0000303|PubMed:32286350};
GN ORFNames=CH063_02829, CH63R_05479;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- BIOTECHNOLOGY: Diterpenoid pyrones display various biological
CC activities and higginsianin A shows anti-HIV activity.
CC {ECO:0000269|PubMed:32286350}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCF42418.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CACQ02005368; CCF42418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; LTAN01000004; OBR09787.1; -; Genomic_DNA.
DR RefSeq; XP_018158304.1; XM_018300454.1.
DR AlphaFoldDB; A0A1B7YCL6; -.
DR SMR; A0A1B7YCL6; -.
DR STRING; 80884.CCF42418; -.
DR EnsemblFungi; CCF42418; CCF42418; CH063_02829.
DR GeneID; 28864561; -.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_6_1; -.
DR OrthoDB; 921996at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR Proteomes; UP000092177; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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 Glycoprotein; Membrane; NAD; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..401
FT /note="Short chain dehydrogenase/reductase dpchH"
FT /id="PRO_0000451553"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 72..80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 99..100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 118..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 275..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 308..310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 401 AA; 43505 MW; 8D9FA383AE9D62D8 CRC64;
MWTGQPASGP PFDHENHSAS CTQHFALFSS PSPANSEPKS MLSAWAHRLC VRAVDVLFGT
FLYVPLGILF LKKSLSGFGD GDWDSSQIPD LHGKVAVVTG GNAGIGYHTV RQLAAKGAKV
YLAARSESRA KEAIKRLREE NPDIPQEKLV WLPLDLSSQA QVVDAARDLM SKTERLDILV
NNAGVDPYNY VKTADGFEMT MAVNHIGHWT LTYCLLPLLK ATAAQQGSDV RVITLSSSGE
RNHSANNHFT TLKDLDDPCA GPGWEDSRLA QGKRYGTSKL ANILFATELQ RRMDEEGAGI
LSLSLNPGTI RTEGAADVMP LVTQPLVWLL FTDAAKGADT TMFAATAREV RENSEQWKGR
YLDGPGRIKP PSPKARDAVA ARNLWNITAA AVKGTGALEK L
