ERG7_GANLU
ID ERG7_GANLU Reviewed; 726 AA.
AC D7NJ68;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Lanosterol synthase {ECO:0000303|PubMed:20460708};
DE EC=5.4.99.7 {ECO:0000250|UniProtKB:P38604};
DE AltName: Full=2,3-epoxysqualene--lanosterol cyclase {ECO:0000250|UniProtKB:P38604};
DE AltName: Full=Oxidosqualene--lanosterol cyclase {ECO:0000250|UniProtKB:P38604};
DE Short=OSC {ECO:0000250|UniProtKB:P38604};
GN Name=LS {ECO:0000303|PubMed:20460708};
OS Ganoderma lucidum (Ling zhi medicinal fungus) (Bracket fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=5315;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND INDUCTION.
RX PubMed=20460708; DOI=10.1271/bbb.90833;
RA Shang C.H., Shi L., Ren A., Qin L., Zhao M.W.;
RT "Molecular cloning, characterization, and differential expression of a
RT lanosterol synthase gene from Ganoderma lucidum.";
RL Biosci. Biotechnol. Biochem. 74:974-978(2010).
RN [2]
RP FUNCTION.
RX PubMed=18051320;
RA Zhao M.W., Liang W.Q., Zhang D.B., Wang N., Wang C.G., Pan Y.J.;
RT "Cloning and characterization of squalene synthase (SQS) gene from
RT Ganoderma lucidum.";
RL J. Microbiol. Biotechnol. 17:1106-1112(2007).
RN [3]
RP FUNCTION.
RX PubMed=29476632; DOI=10.1002/bit.26583;
RA Wang W.F., Xiao H., Zhong J.J.;
RT "Biosynthesis of a ganoderic acid in Saccharomyces cerevisiae by expressing
RT a cytochrome P450 gene from Ganoderma lucidum.";
RL Biotechnol. Bioeng. 115:1842-1854(2018).
CC -!- FUNCTION: Lanosterol synthase; part of the third module of ergosterol
CC biosynthesis pathway that includes the late steps of the pathway (By
CC similarity). The third module or late pathway involves the ergosterol
CC synthesis itself through consecutive reactions that mainly occur in the
CC endoplasmic reticulum (ER) membrane (By similarity). Firstly, the
CC squalene synthase SQS catalyzes the condensation of 2 farnesyl
CC pyrophosphate moieties to form squalene, which is the precursor of all
CC steroids (PubMed:18051320). Secondly, the squalene epoxidase catalyzes
CC the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene,
CC which is considered to be a rate-limiting enzyme in steroid
CC biosynthesis (By similarity). Then, the lanosterol synthase LS
CC catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a
CC reaction that forms the sterol core (PubMed:20460708). In the next
CC steps, lanosterol is transformed to ergosterol via a complex process
CC involving various demethylation, reduction and desaturation reactions
CC (By similarity). Lanosterol is also an intermediate in the biosynthesis
CC of triterpenes such as ganoderic acids (GA), a group of highly
CC oxygenated lanostane-type triterpenoids which are well recognized as a
CC main group of unique bioactive compounds in the medicinal mushroom
CC Ganoderma lucidum (Probable). {ECO:0000250|UniProtKB:P38604,
CC ECO:0000269|PubMed:18051320, ECO:0000269|PubMed:20460708,
CC ECO:0000305|PubMed:29476632}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = lanosterol; Xref=Rhea:RHEA:14621,
CC ChEBI:CHEBI:15441, ChEBI:CHEBI:16521; EC=5.4.99.7;
CC Evidence={ECO:0000250|UniProtKB:P38604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14622;
CC Evidence={ECO:0000250|UniProtKB:P38604};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 3/3. {ECO:0000250|UniProtKB:P38604}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:P38604}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38604};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P38604}.
CC -!- INDUCTION: Expression is up-regulated by methyl jasmonate (MeJA).
CC {ECO:0000269|PubMed:20460708}.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {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; GQ169528; ADD60469.1; -; mRNA.
DR EMBL; GQ169529; ADD60470.1; -; Genomic_DNA.
DR SMR; D7NJ68; -.
DR BRENDA; 5.4.99.7; 2399.
DR UniPathway; UPA00767; UER00753.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016866; F:intramolecular transferase activity; IEA:InterPro.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd02892; SQCY_1; 1.
DR InterPro; IPR032696; SQ_cyclase_C.
DR InterPro; IPR032697; SQ_cyclase_N.
DR InterPro; IPR018333; Squalene_cyclase.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11764; PTHR11764; 1.
DR Pfam; PF13243; SQHop_cyclase_C; 1.
DR Pfam; PF13249; SQHop_cyclase_N; 1.
DR SFLD; SFLDG01016; Prenyltransferase_Like_2; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR TIGRFAMs; TIGR01787; squalene_cyclas; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Isomerase; Lipid biosynthesis; Lipid droplet;
KW Lipid metabolism; Membrane; Repeat; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..726
FT /note="Lanosterol synthase"
FT /id="PRO_0000454394"
FT REPEAT 123..164
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 482..524
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 559..599
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 608..657
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT REPEAT 666..713
FT /note="PFTB 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 454
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 726 AA; 82876 MW; B41343B455B186E1 CRC64;
MAAYAPLELP ASGALPFTDY ARWRLRLSPN GDHTWHYLRT DDEVAAWPQS TYDKYWLGQD
VGLPELPPPT NALEAARNGY RFFQKHQTER GHWAGEYGGP MFLLPGLVIG SYVCGMGFKT
EERLEMIRYL FNHVNEDGGW GIHIEGPSTV FGTALNYCAA RILGLKADHP VAVKARACLH
KLGGAVGIPS WGKFWLSILN VYDWEGNHPI PSELWLLPDW VPIHPHRWWI HTRNVYIPMG
YLYGVRFKME ENELVSSLRQ ELYTTNYYSI DWPAQRSNVA AVDLYTPHSA VLEGLYTLLG
AYESCALPPL RRAAIRRCYE LVVLEDENTD CQDLGPVNKM MNQIVRVHAE GRESAGAKRH
LERRHDFMWM GAEGMMMCGT NGSQLWDIGF MAQALIETGL GAEDEFRESA LRALQWLDNC
QIRENPKHYR TAYRHQTKGA WPFSTKTQGY TVSDCTGEGL KAVLYLQEHV KGAPKLISER
RLCDAVDVLL SLQNTDGGFA SYELIRAPQW MEWLNPAEVF GNIMTEFNYP ECTTSVITAL
AIFRKHYPHY RTADIQRTIT HAVDYLHKAQ RPEGGWFGSW GICFTYATQF ALESLALVGE
TYETSAASRR ACEFLVSKQR ADGGWGESYK ACEVIEWVEH KDTQVVQTCW AAMALMYAKY
PHPEPIERAV KLVMSRQRPD GSWPQEAIEG VFNKNVAISY PNFKFEFTIW MLGRAHRYLK
ELHAKK
