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 02-OCT-2024, entry version 19. 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; Pentapetalae; OC asterids; campanulids; Apiales; Araliaceae; Panax. OX NCBI_TaxID=4054; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND INDUCTION BY METHYL 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., Wang L., RA 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 adventitious RT 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 biosynthesis."; RL Molecules 23:0-0(2018). CC -!- FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or CC panaxosides) and phytosterols biosynthetic pathways (PubMed:27746309, CC PubMed:29378087). Catalyzes the biosynthesis of squalene (By CC 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 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: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 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: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 from CC farnesyl diphosphate: step 1/3. {ECO:0000250|UniProtKB:P53799}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000250|UniProtKB:P53799}. CC -!- INDUCTION: Induced methyl jasmonate (MeJA) in adventitious roots CC (PubMed:25642758). Induced by A.niger mycelium-derived elicitor, thus CC improving ginsenosides production in adventitious roots culture CC (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 AlphaFoldDB; A0A1P7Y0C9; -. DR SMR; A0A1P7Y0C9; -. DR UniPathway; UPA00767; UER00751. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:TreeGrafter. DR GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro. DR GO; GO:0051996; F:squalene synthase activity; IEA:UniProtKB-EC. DR GO; GO:0045338; P:farnesyl diphosphate metabolic process; IEA:TreeGrafter. 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; Farnesyl Diphosphate Synthase; 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 NCBIfam; TIGR01559; squal_synth; 1. DR PANTHER; PTHR11626; FARNESYL-DIPHOSPHATE FARNESYLTRANSFERASE; 1. DR PANTHER; PTHR11626:SF2; SQUALENE SYNTHASE; 1. DR Pfam; PF00494; SQS_PSY; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 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 FT /note="Squalene synthase 8" FT /id="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 //