ERIG_HERER
ID ERIG_HERER Reviewed; 306 AA.
AC A0A1V0QSF1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Polyprenyl transferase eriG {ECO:0000303|PubMed:28371074};
DE EC=2.5.1.- {ECO:0000269|PubMed:28371074, ECO:0000269|PubMed:31535864};
DE AltName: Full=Erinacine biosynthesis cluster protein G {ECO:0000303|PubMed:28371074};
GN Name=eriG {ECO:0000303|PubMed:28371074};
OS Hericium erinaceus (Lion's mane mushroom) (Hydnum erinaceus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Hericiaceae; Hericium.
OX NCBI_TaxID=91752;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, FUNCTION, AND PATHWAY.
RX PubMed=28371074; DOI=10.1002/anie.201700565;
RA Yang Y.L., Zhang S., Ma K., Xu Y., Tao Q., Chen Y., Chen J., Guo S.,
RA Ren J., Wang W., Tao Y., Yin W.B., Liu H.;
RT "Discovery and characterization of a new family of diterpene cyclases in
RT bacteria and fungi.";
RL Angew. Chem. Int. Ed. 56:4749-4752(2017).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=31535864; DOI=10.1021/jacs.9b08935;
RA Liu C., Minami A., Ozaki T., Wu J., Kawagishi H., Maruyama J.I., Oikawa H.;
RT "Efficient reconstitution of basidiomycota diterpene erinacine gene cluster
RT in ascomycota host Aspergillus oryzae based on genomic DNA sequences.";
RL J. Am. Chem. Soc. 141:15519-15523(2019).
CC -!- FUNCTION: Polyprenyl transferase; part of the gene cluster that
CC mediates the biosynthesis of erinacines, cyathane-xylosides that show
CC unique biological activities, including leishmanicidal activity,
CC stimulating activity for nerve growth-factor synthesis, and agonistic
CC activity toward the kappa opioid receptor (PubMed:31535864). The
CC geranylgeranyl diphosphate (GGPP) synthase eriE catalyzes the first
CC step in erinacines biosynthesis via conversion of farnesyl
CC pyrophosphate and isopentyl pyrophosphate into geranylgeranyl
CC pyrophosphate (GGPP) (PubMed:31535864). GGPP is then substrate of the
CC diterpene cyclase eriG for the production of cyatha-3,12-diene
CC (PubMed:28371074). EriG is unable to use geranyl diphosphate (GPP) or
CC farnesyl diphosphate (FPP) as substrates (PubMed:28371074). The
CC cytochrome P450 monooxygenase eriI then hydroxylates cyatha-3,12-diene
CC at C-14 of the seven-membered ring to produce erinacol, which is
CC further hydroxylated at C-15 by the cytochrome P450 monooxygenase eriC
CC to yield cyathadiol (PubMed:31535864). The cytochrome P450
CC monooxygenase eriA then catalyzes C-11 hydroxylation in the presence of
CC the short chain dehydrogenase/reductase (SDR) eriH, which leads to the
CC production of cyathatriol (PubMed:31535864). The acetyltransferase eriL
CC converts cyathatriol into 11-O-acetyl-cyathatriol (PubMed:31535864).
CC The SDR eriH catalyzes further oxidation of 11-O-acetyl-cyathatriol
CC into 1-O-acetylcyathin A3 (PubMed:31535864). Finally, the glycosyl
CC transferase eriJ tranfers xylose from UDP-xylose onto C-14 of 11-O-
CC acetyl-cyathatriol to form eracine Q (PubMed:31535864). EriJ is also
CC able to convert 11-O-acetyl-cyathatriol to eracine Q2 by using UDP-D-
CC glucose as cosubstrate, but at a lower rate (PubMed:31535864). In the
CC absence of eriL and eriJ, the SDR eriH is able to convert cyathatriol
CC to cyathin A3; this is likely a switching mechanism in the biosynthesis
CC of cyathins (C-14 ketogroup)and erinacines (C-14 glycosylated group)
CC (PubMed:31535864). The roles of the SDR eriB, the polyprenyl
CC transferase eriF and the dehydrogenase eriK have still to be identified
CC (Probable). {ECO:0000269|PubMed:28371074, ECO:0000269|PubMed:31535864,
CC ECO:0000305|PubMed:31535864}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28371074};
CC -!- ACTIVITY REGULATION: EDTA completely blocks the reaction.
CC {ECO:0000269|PubMed:28371074}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=99.6 uM for GGPP {ECO:0000269|PubMed:28371074};
CC Vmax=4.0 nmol/min/mg enzyme {ECO:0000269|PubMed:28371074};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:28371074, ECO:0000269|PubMed:31535864}.
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; KY683782; ARE72244.1; -; mRNA.
DR AlphaFoldDB; A0A1V0QSF1; -.
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 Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR Pfam; PF01040; UbiA; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..306
FT /note="Polyprenyl transferase eriG"
FT /id="PRO_0000452925"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 306 AA; 33916 MW; 2AB9E7EBB2E4B0CF CRC64;
MSVFAPIARE LDIFFGFSWR DWSTTIIPGS IFAVGAMRDL PPATLVKNYL FLVTWLTPYI
YFFNLSNQIT GVDEDKINKP DRPIPSGKVT LQGAQRRWIA AFSTFLGIAL YQPEFLPETL
CWIATVAFLC LTSYGDHWFG KNCVAMTTGT WALLSASWKA IAPATPTSDA WVYAVSVWAG
LITHIQDLRD MEGDKAVGRK TLPLVFGDMG SRLIITFFAL PAACWVLSLA GIFQLAPVTL
GALHAILGYR VLRQGGPRYD HKTYMFYTYI FCLILAFCAL DGLGLKINAE SLRALLATTG
VSLKEL
