SQS3_PANGI
ID SQS3_PANGI Reviewed; 415 AA.
AC D2K762;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Squalene synthase 3 {ECO:0000303|PubMed:29509695, ECO:0000303|Ref.1};
DE Short=PgSS3 {ECO:0000303|PubMed:29509695, ECO:0000303|Ref.1};
DE Short=SQS 3 {ECO:0000305};
DE EC=2.5.1.21 {ECO:0000250|UniProtKB:P53799};
DE AltName: Full=FPP:FPP farnesyltransferase SS3 {ECO:0000305};
DE AltName: Full=Farnesyl-diphosphate farnesyltransferase SS3 {ECO:0000305};
GN Name=SS3 {ECO:0000303|Ref.1};
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 [MRNA].
RA Kim T.D., Han J.Y., Choi Y.E.;
RT "Isolation and characterization of squalene synthase gene (PgSS3) in Panax
RT ginseng.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP REVIEW, AND NOMENCLATURE.
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:29378087).
CC Catalyzes the biosynthesis of squalene (By similarity).
CC {ECO:0000250|UniProtKB:O48666, 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:0000303|PubMed:29509695};
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:0000303|PubMed:29509695};
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 membrane
CC {ECO:0000250|UniProtKB:P53799}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; GU183406; ACZ71037.1; -; mRNA.
DR AlphaFoldDB; D2K762; -.
DR SMR; D2K762; -.
DR UniPathway; UPA00767; UER00751.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProt.
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; Membrane; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..415
FT /note="Squalene synthase 3"
FT /id="PRO_0000446954"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 415 AA; 47121 MW; 1B343E02D9D1C0EE 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
EDLKYEENSG KAVQCLNDMV TNALLHVEDC LKYMSDLRDP AIFRFCAIPQ IMAIGTLALC
YNNIQVFRGV VKMRRGLTAK VIDRTNTMSD VYGTFFDFSC MLKSKVDNND PNATKTLSRL
EAIQKICKNS GALTTKRKSY IIENESGYNS TLIIILFIIL AILYAYLSSN LPNSL
