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   25-MAY-2022, entry version 14.
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}.
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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:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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: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; 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; 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