SUBC_METRA
ID SUBC_METRA Reviewed; 109 AA.
AC A0A0B2XGM8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Polyprenyl transferase subC {ECO:0000303|PubMed:27189118};
DE EC=2.5.1.- {ECO:0000269|PubMed:27189118};
DE AltName: Full=Subglutinol biosynthesis cluster protein C {ECO:0000303|PubMed:27189118};
GN Name=subC {ECO:0000303|PubMed:27189118}; ORFNames=MAA_11696;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=27189118; DOI=10.1038/ja.2016.54;
RA Kato H., Tsunematsu Y., Yamamoto T., Namiki T., Kishimoto S., Noguchi H.,
RA Watanabe K.;
RT "New natural products isolated from Metarhizium robertsii ARSEF 23 by
RT chemical screening and identification of the gene cluster through
RT engineered biosynthesis in Aspergillus nidulans A1145.";
RL J. Antibiot. 69:561-566(2016).
CC -!- FUNCTION: Polyprenyl transferase; part of the gene cluster that
CC mediates the biosynthesis of the immunosuppressants subglutinols,
CC meroterpenoids consisting of an alpha-pyrone (4-hydroxy-5,6-dimethyl-2-
CC pyrone) moiety attached to a decalin core fused to a five-membered
CC cyclic ether carrying a prenylside chain (PubMed:27189118). The first
CC step of the pathway is the synthesis of the alpha-pyrone moiety by the
CC polyketide synthase subA via condensation of one acetyl-CoA starter
CC unit with 3 malonyl-CoA units and 2 methylations (PubMed:27189118). The
CC alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP)
CC formed by the GGPP synthase subD through the action of the
CC prenyltransferase subC to yield a linear alpha-pyrone diterpenoid
CC (PubMed:27189118). Subsequent steps in the subglutinol biosynthetic
CC pathway involve the decalin core formation, which is thought to be
CC initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent
CC oxidoreductase subE (Probable). The following cyclization cascade would
CC be catalyzed by the terpene cyclase subB (Probable). Lastly, the FAD-
CC dependent dehydrogenase subF probably catalyzes the five-membered
CC cyclic ether formation to complete the formation of subglutinol A
CC (Probable). Subsequent redox reactions appear to give rise to
CC subglutinol C and D, however, it remains unclear which enzymes are
CC responsible for these transformations (Probable).
CC {ECO:0000269|PubMed:27189118, ECO:0000305|PubMed:27189118}.
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:0000269|PubMed:27189118}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; ADNJ02000014; KHO10692.1; -; Genomic_DNA.
DR RefSeq; XP_011410913.1; XM_011412611.1.
DR AlphaFoldDB; A0A0B2XGM8; -.
DR SMR; A0A0B2XGM8; -.
DR EnsemblFungi; KHO10692; KHO10692; MAA_11696.
DR GeneID; 23633144; -.
DR KEGG; maj:MAA_11696; -.
DR HOGENOM; CLU_147528_0_0_1; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
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 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; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..109
FT /note="Polyprenyl transferase subC"
FT /id="PRO_0000451339"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 109 AA; 11862 MW; 1E032B892630B89B CRC64;
MPTSANKVET AWSALLAGAA ETRQEHLAPS PLFILRQTLF CVLAAYLFCG AGMVWNDWID
RDIDANVART KNRPLASGKV TTAQAFVWMA LQVIASCAVL HVMLDGKDV
