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 10-FEB-2021, entry version 13. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 Proteomes; UP000092177; Unassembled WGS sequence. 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 NP_BIND 72..80 FT /note="NAD" FT /evidence="ECO:0000250|UniProtKB:Q92506" FT NP_BIND 99..100 FT /note="NAD" FT /evidence="ECO:0000250|UniProtKB:Q92506" FT NP_BIND 118..120 FT /note="NAD" FT /evidence="ECO:0000250|UniProtKB:Q92506" FT NP_BIND 275..279 FT /note="NAD" FT /evidence="ECO:0000250|UniProtKB:Q92506" FT NP_BIND 308..310 FT /note="NAD" FT /evidence="ECO:0000250|UniProtKB:Q92506" FT ACT_SITE 275 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" 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 //