ID SQS8_PANGI Reviewed; 391 AA. AC A0A1P7Y0C9; DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2017, sequence version 1. DT 31-JUL-2019, entry version 9. DE RecName: Full=Squalene synthase 8 {ECO:0000303|PubMed:25642758}; DE Short=PgSS8 {ECO:0000305}; DE Short=SQS 8 {ECO:0000305}; DE EC=2.5.1.21 {ECO:0000250|UniProtKB:P53799}; DE AltName: Full=FPP:FPP farnesyltransferase SS8 {ECO:0000305}; DE AltName: Full=Farnesyl-diphosphate farnesyltransferase SS8 {ECO:0000305}; GN Name=SS8 {ECO:0000303|PubMed:25642758}; OS Panax ginseng (Korean ginseng). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Apiales; Araliaceae; Panax. OX NCBI_TaxID=4054; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND INDUCTION BY METYL RP JASMONATE. RC STRAIN=cv. Damaya; RX PubMed=25642758; DOI=10.3390/ijms16023035; RA Cao H., Nuruzzaman M., Xiu H., Huang J., Wu K., Chen X., Li J., RA Wang L., Jeong J.-H., Park S.-J., Yang F., Luo J., Luo Z.; RT "Transcriptome analysis of methyl jasmonate-elicited Panax ginseng RT adventitious roots to discover putative ginsenoside biosynthesis and RT transport genes."; RL Int. J. Mol. Sci. 16:3035-3057(2015). RN [2] RP FUNCTION, AND INDUCTION BY ASPERGILLUS NIGER. RX PubMed=27746309; DOI=10.1016/j.jbiotec.2016.10.011; RA Li J., Liu S., Wang J., Li J., Liu D., Li J., Gao W.; RT "Fungal elicitors enhance ginsenosides biosynthesis, expression of RT functional genes as well as signal molecules accumulation in RT adventitious roots of Panax ginseng C. A. Mey."; RL J. Biotechnol. 239:106-114(2016). RN [3] RP REVIEW. RX PubMed=29378087; DOI=10.1002/bab.1649; RA Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.; RT "Advances in ginsenoside biosynthesis and metabolic regulation."; RL Biotechnol. Appl. Biochem. 65:514-522(2018). RN [4] RP REVIEW. RX PubMed=29509695; DOI=10.3390/molecules23030589; RA Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.; RT "Progress on the studies of the key enzymes of ginsenoside RT biosynthesis."; RL Molecules 23:0-0(2018). CC -!- FUNCTION: Component of the triterpene saponins (e.g. ginsenosides CC or panaxosides) and phytosterols biosynthetic pathways CC (PubMed:27746309, PubMed:29378087). Catalyzes the biosynthesis of CC squalene (By similarity). {ECO:0000250|UniProtKB:O48666, CC ECO:0000269|PubMed:27746309, ECO:0000303|PubMed:29378087}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 CC diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:32299, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; CC EC=2.5.1.21; Evidence={ECO:0000250|UniProtKB:P53799}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32300; CC Evidence={ECO:0000250|UniProtKB:D2K762}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 CC diphosphate + NADP(+) + squalene; Xref=Rhea:RHEA:32295, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; CC EC=2.5.1.21; Evidence={ECO:0000250|UniProtKB:P53799}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32296; CC Evidence={ECO:0000250|UniProtKB:D2K762}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P53799}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P53799}; CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol CC from farnesyl diphosphate: step 1/3. CC {ECO:0000250|UniProtKB:P53799}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000250|UniProtKB:P53799}. CC -!- INDUCTION: Induced metyl jasmonate (MeJA) in adventitious roots CC (PubMed:25642758). Induced by A.niger mycelium-derived elicitor, CC thus improving ginsenosides production in adventitious roots CC culture (PubMed:27746309). {ECO:0000269|PubMed:25642758, CC ECO:0000269|PubMed:27746309}. CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase 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; KP689318; AJK30630.1; -; mRNA. DR EMBL; KP689319; AJK30631.1; -; mRNA. DR SMR; A0A1P7Y0C9; -. DR UniPathway; UPA00767; UER00751. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. 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:0006696; P:ergosterol biosynthetic process; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB. DR GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB. 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; IPR033904; Trans_IPPS_HH. DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR TIGRFAMs; TIGR01559; squal_synth; 1. DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1. DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1. PE 2: Evidence at transcript level; KW Endoplasmic reticulum; Isoprene biosynthesis; Magnesium; KW Multifunctional enzyme; NADP; Transferase. FT CHAIN 1 391 Squalene synthase 8. FT /FTId=PRO_0000446955. SQ SEQUENCE 391 AA; 44481 MW; 0F7F3A563FD87AB1 CRC64; MGSLGAILKH PDDFYPLLKL KIAARHAEKQ IPSEPHWAFC YSMLHKVSRS FGLVIQQLGP QLRDAVCIFY LVLRALDTVE DDTSISTEVK VPIVMAFHCH IYDNDWHFSC GTKEYKVLMD EFHHVSNAFL DLGSSYKEAI EDITMRMGAG MAKFICKEVE TIDDYDEYCH YVAGLVGLGL SKLFHASGAE DLATDSLSNS MGLFLQKTNI IRDYLEDINE IPKSRMFWPR QIWSKYVDKL EDLKYEENSA KAVQCLNDMV TDALVHAEDC LKYMSDLRGP AIFRFCAIPQ IMAIGTLALC FNNTQVFRGV VKMRRGLTAK VIDQTKTMSD VYGAFFDFSC LLKSKVDNND PNATKTLSRL EAIQKTCKES GTLSKRFCVF DFPLETIFYR V //