ERIL_HERER
ID ERIL_HERER Reviewed; 382 AA.
AC P0DO28;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 25-MAY-2022, entry version 4.
DE RecName: Full=Acetyltransferase eriL {ECO:0000303|PubMed:31535864};
DE EC=2.3.1.- {ECO:0000269|PubMed:31535864};
DE AltName: Full=Erinacine biosynthesis cluster protein L {ECO:0000303|PubMed:31535864};
GN Name=eriL {ECO:0000303|PubMed:31535864};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP 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).
RN [2]
RP FUNCTION.
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).
CC -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC biosynthesis of erinacines, cyathane-xylosides that show unique
CC biological activities, including leishmanicidal activity, stimulating
CC activity for nerve growth-factor synthesis, and agonistic activity
CC toward the kappa opioid receptor (PubMed:31535864). The geranylgeranyl
CC diphosphate (GGPP) synthase eriE catalyzes the first step in erinacines
CC biosynthesis via conversion of farnesyl pyrophosphate and isopentyl
CC pyrophosphate into geranylgeranyl pyrophosphate (GGPP)
CC (PubMed:31535864). GGPP is then substrate of the diterpene cyclase eriG
CC for the production of cyatha-3,12-diene (PubMed:28371074). EriG is
CC unable to use geranyl diphosphate (GPP) or farnesyl diphosphate (FPP)
CC as substrates (PubMed:28371074). The cytochrome P450 monooxygenase eriI
CC then hydroxylates cyatha-3,12-diene at C-14 of the seven-membered ring
CC to produce erinacol, which is further hydroxylated at C-15 by the
CC cytochrome P450 monooxygenase eriC to yield cyathadiol
CC (PubMed:31535864). The cytochrome P450 monooxygenase eriA then
CC catalyzes C-11 hydroxylation in the presence of the short chain
CC dehydrogenase/reductase (SDR) eriH, which leads to the production of
CC cyathatriol (PubMed:31535864). The acetyltransferase eriL converts
CC cyathatriol into 11-O-acetyl-cyathatriol (PubMed:31535864). The SDR
CC eriH catalyzes further oxidation of 11-O-acetyl-cyathatriol into 1-O-
CC acetylcyathin A3 (PubMed:31535864). Finally, the glycosyl transferase
CC eriJ tranfers xylose from UDP-xylose onto C-14 of 11-O-acetyl-
CC cyathatriol to form eracine Q (PubMed:31535864). EriJ is also able to
CC convert 11-O-acetyl-cyathatriol to eracine Q2 by using UDP-D-glucose as
CC cosubstrate, but at a lower rate (PubMed:31535864). In the absence of
CC eriL and eriJ, the SDR eriH is able to convert cyathatriol to cyathin
CC A3; this is likely a switching mechanism in the biosynthesis of
CC 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31535864}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the wax synthase family. {ECO:0000305}.
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DR AlphaFoldDB; P0DO28; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR InterPro; IPR044851; Wax_synthase.
DR InterPro; IPR032805; Wax_synthase_dom.
DR PANTHER; PTHR31595; PTHR31595; 1.
DR Pfam; PF13813; MBOAT_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..382
FT /note="Acetyltransferase eriL"
FT /id="PRO_0000452929"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 382 AA; 43793 MW; 6B1551370C3AEDA4 CRC64;
MSTTLQPLPG GLQVAVQACL FLGAVSRSRR FRALLFPPVL AMSLYMLLYT TTGKDSDDIV
TWSLITTSLL QGSDILLIND VADLRLVGQK TPTNELSLWQ RIKWAGRLMS APRAVGFTHE
SRHVFPPHPP ANEPRWTFIK RQSLTTLFYF VVLDLVHTFI VLSPVFQRDG VSLTSVDWPM
RFLYTALHAA HLWSYMSFGY SAASVVLVAL GVSDSDQWPA IYGDWSNAYT IRRFWGRVWH
QVFRRIVSTH GDFVTYRFLA LPKGTFFADN VHRYTAFFIS GVIHAVGEYG MFRDQWLQKS
GALRFFLLQA TAILVEQEVG KIFKLQPTPL LRRLGYMWTF LWFVFTLPHW MDPQFRQGMA
DNYGFPLSVS YGLLKGQWRL VA
