DPCHC_COLHI
ID DPCHC_COLHI Reviewed; 316 AA.
AC A0A1B7YCK2; H1VQB3;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Polyprenyl transferase dpchC {ECO:0000303|PubMed:32286350};
DE EC=2.5.1.- {ECO:0000305|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein C {ECO:0000303|PubMed:32286350};
GN Name=dpchC {ECO:0000303|PubMed:32286350};
GN ORFNames=CH063_02830, CH63R_05478;
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, 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: Polyprenyl transferase; part of the gene cluster that
CC mediates the biosynthesis of the diterpenoid pyrones higginsianins A
CC and B (PubMed:32286350). The first step of the pathway is the synthesis
CC of the alpha-pyrone moiety by the polyketide synthase dpchA via
CC condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units
CC and 2 methylations (Probable). The alpha-pyrone is then combined with
CC geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD
CC through the action of the prenyltransferase dpchC to yield a linear
CC 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P32378};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:32286350}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-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 -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCF42419.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CACQ02005368; CCF42419.1; ALT_SEQ; Genomic_DNA.
DR EMBL; LTAN01000004; OBR09786.1; -; Genomic_DNA.
DR RefSeq; XP_018158303.1; XM_018300453.1.
DR AlphaFoldDB; A0A1B7YCK2; -.
DR SMR; A0A1B7YCK2; -.
DR STRING; 80884.CCF42419; -.
DR EnsemblFungi; CCF42419; CCF42419; CH063_02830.
DR GeneID; 28864560; -.
DR eggNOG; KOG1381; Eukaryota.
DR HOGENOM; CLU_075330_0_0_1; -.
DR OrthoDB; 1343847at2759; -.
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:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..316
FT /note="Polyprenyl transferase dpchC"
FT /id="PRO_0000451533"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 316 AA; 35448 MW; 9EA58F0555BFF751 CRC64;
MAATKDRQLF RHLLRLSRFD RYNPLFTTFA GLWSTLLAGG AKMAEQRSDM SVATVFQQCA
LCFVASYLFC GAGMVWNDWI DRDIDANVAR TKERPLASGK VTATEAMVWM VLQAALSWGV
LEVMLDGKDV AKHFIPVAAA SVLYPFGKRS LARMLGIYPQ YILAFTIAWP AVIGRAAIYG
QYESYAETLR QCLPLCTMVF FWTIYLNTAY SYQDVVDDRK LGVNSFYNIA GKHIHLLLVA
LVSPILVCLP IYLFELHSLW LWLSWMGVWT ASLAQQLVQF DPKQPASGGS IHRSNFILGI
WTILACVVQV FLTGSA
