ERG9_GANLU
ID ERG9_GANLU Reviewed; 467 AA.
AC A0SJQ5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Squalene synthase {ECO:0000303|PubMed:18051320};
DE Short=SQS {ECO:0000303|PubMed:18051320};
DE Short=SS {ECO:0000250|UniProtKB:P29704};
DE EC=2.5.1.21 {ECO:0000305|PubMed:18051320};
DE AltName: Full=FPP:FPP farnesyltransferase {ECO:0000250|UniProtKB:P29704};
DE AltName: Full=Farnesyl-diphosphate farnesyltransferase {ECO:0000250|UniProtKB:P29704};
GN Name=SQS {ECO:0000303|PubMed:18051320};
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], AND 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 [2]
RP DEVELOPMENTAL STAGE.
RA Zhao M., Zhong J., Liang W.;
RT "Analysis of squalene synthase expression during the development of
RT Ganoderma lucidum.";
RL J. Microbiol. Biotechnol. 14:116-120(2004).
RN [3]
RP FUNCTION.
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 [4]
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).
RN [5]
RP INDUCTION.
RX PubMed=30821132; DOI=10.1111/1751-7915.13381;
RA Xu J.W., Yue T.H., Yu X., Zhao P., Li T., Li N.;
RT "Enhanced production of individual ganoderic acids by integrating
RT Vitreoscilla haemoglobin expression and calcium ion induction in liquid
RT static cultures of Ganoderma lingzhi.";
RL Microb. Biotechnol. 12:1180-1187(2019).
CC -!- FUNCTION: Squalene 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:P29704,
CC ECO:0000269|PubMed:18051320, ECO:0000269|PubMed:20460708,
CC ECO:0000305|PubMed:29476632}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate
CC + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC Evidence={ECO:0000305|PubMed:18051320};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32296;
CC Evidence={ECO:0000305|PubMed:18051320};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate +
CC NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC Evidence={ECO:0000305|PubMed:18051320};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32300;
CC Evidence={ECO:0000305|PubMed:18051320};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P29704};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 1/3. {ECO:0000250|UniProtKB:P29704}.
CC -!- DEVELOPMENTAL STAGE: Expression is relatively low in mycelia and
CC reaches the highest level in the primordia. {ECO:0000269|Ref.2}.
CC -!- INDUCTION: Expression is induced in ganoderic acid (GA) producing
CC conditions. {ECO:0000269|PubMed:30821132}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; DQ494674; ABF57213.1; -; mRNA.
DR EMBL; DQ494675; ABF57214.1; -; Genomic_DNA.
DR SMR; A0SJQ5; -.
DR BRENDA; 2.5.1.21; 2399.
DR UniPathway; UPA00767; UER00751.
DR GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051996; F:squalene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR CDD; cd00683; Trans_IPPS_HH; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR InterPro; IPR006449; Squal_synth-like.
DR InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR InterPro; IPR044844; Trans_IPPS_euk-type.
DR InterPro; IPR033904; Trans_IPPS_HH.
DR PANTHER; PTHR11626; PTHR11626; 1.
DR Pfam; PF00494; SQS_PSY; 1.
DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR TIGRFAMs; TIGR01559; squal_synth; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 2: Evidence at transcript level;
KW Transferase.
FT CHAIN 1..467
FT /note="Squalene synthase"
FT /id="PRO_0000454393"
SQ SEQUENCE 467 AA; 54018 MW; 61B06C6C88750EB8 CRC64;
MGATSMLTLL LTHPFEFRVL IQYKLWHEPK RDITQVSEHP TSGWDRPTMR RCWEFLDQTS
RSFSGVIKEV EGDLARVICL FYLVLRGLDT IEDDMTLPDE KKQPILRQFH KLAVKPGWTF
DECGPKEKDR QLLVEWTVVS EELNRLDACY RDIIIDIAEK MQTGMADYAH KAATTNSIYI
GTVDEYNLYC HYVAGLVGEG LTRFWAASGK EAEWLGDQLE LTNAMGLMLQ KTNIIRDFRE
DAEERRFFWP REIWGRDAYG KAVGRANGFR EMHELYERGN EKQALWVQSG MVVDVLGHAT
DSLDYLRLLT KQSIFCFCAI PQTMAMATLS LCFMNYDMFH NHIKIRRAEA ASLIMRSTNP
RDVAYIFRDY ARKMHARALP EDPSFLRLSV ACGKIEQWCE RHYPSFVRLQ QVSGGGIVFD
PSDARTKVVE AAQARDNELA REKRLAELRD KTGKLERKLR WSQAPSS
